______
Publications
2024
Lindner, Sandra; Bonin, Martin; Hellmann, Margareta J.; Moerschbacher, Bruno M.
Three intertwining effects guide the mode of action of chitin deacetylase de- and N-acetylation reactions Journal Article
In: Carbohydrate Polymers, vol. 347, pp. 122725, 2024, ISSN: 0144-8617.
@article{LINDNER2025122725,
title = {Three intertwining effects guide the mode of action of chitin deacetylase de- and N-acetylation reactions},
author = {Sandra Lindner and Martin Bonin and Margareta J. Hellmann and Bruno M. Moerschbacher},
url = {https://www.sciencedirect.com/science/article/pii/S0144861724009512},
doi = {https://doi.org/10.1016/j.carbpol.2024.122725},
issn = {0144-8617},
year = {2024},
date = {2024-09-23},
urldate = {2025-01-01},
journal = {Carbohydrate Polymers},
volume = {347},
pages = {122725},
abstract = {Chitosans are promising multi-functional biomolecules for various applications whose performance is dependent on three key structural parameters, including the pattern of acetylation (PA). To date, chitin deacetylases (CDAs) are the only tool to control the PA of chitosan polymers via their specific mode of action during de- or N-acetylation. For a start, this review summarizes the current state of research on the classification of carbohydrate esterase 4 enzymes, the features in sequence and structure of CDAs, and the different PAs produced by different CDAs during de- or N-acetylation. In the main part, we introduce three effects that guide the mode of action of these enzymes: the already established subsite capping effect, the subsite occupation effect, and the subsite preference effect. We show how their interplay controls the PA of CDA products and describe their molecular basis. For one thing, this review aims to equip the reader with the knowledge to understand and analyze CDAs – including a guide for in silico and in vitro analyses. But more importantly, we intend to reform and extend the model explaining their mode of action on chitosans to facilitate a deeper understanding of these important enzymes for biology and biotechnology.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Chitosans are promising multi-functional biomolecules for various applications whose performance is dependent on three key structural parameters, including the pattern of acetylation (PA). To date, chitin deacetylases (CDAs) are the only tool to control the PA of chitosan polymers via their specific mode of action during de- or N-acetylation. For a start, this review summarizes the current state of research on the classification of carbohydrate esterase 4 enzymes, the features in sequence and structure of CDAs, and the different PAs produced by different CDAs during de- or N-acetylation. In the main part, we introduce three effects that guide the mode of action of these enzymes: the already established subsite capping effect, the subsite occupation effect, and the subsite preference effect. We show how their interplay controls the PA of CDA products and describe their molecular basis. For one thing, this review aims to equip the reader with the knowledge to understand and analyze CDAs – including a guide for in silico and in vitro analyses. But more importantly, we intend to reform and extend the model explaining their mode of action on chitosans to facilitate a deeper understanding of these important enzymes for biology and biotechnology.
Hellmann, Margareta J; Gillet, Dominique; Trombotto, Stéphane; Raetz, Sonja; Moerschbacher, Bruno M; Cord-Landwehr, Stefan
Heterogeneously deacetylated chitosans possess an unexpected regular pattern favoring acetylation at every third position Journal Article
In: Nat Commun, vol. 15, no. 1, pp. 6695, 2024, ISSN: 2041-1723.
@article{pmid39107282,
title = {Heterogeneously deacetylated chitosans possess an unexpected regular pattern favoring acetylation at every third position},
author = {Margareta J Hellmann and Dominique Gillet and Stéphane Trombotto and Sonja Raetz and Bruno M Moerschbacher and Stefan Cord-Landwehr},
doi = {10.1038/s41467-024-50857-1},
issn = {2041-1723},
year = {2024},
date = {2024-08-01},
journal = {Nat Commun},
volume = {15},
number = {1},
pages = {6695},
abstract = {Chitosans are promising biopolymers for diverse applications, with material properties and bioactivities depending i.a. on their pattern of acetylation (PA). Commercial chitosans are typically produced by heterogeneous deacetylation of chitin, but whether this process yields chitosans with a random or block-wise PA has been debated for decades. Using a combination of recently developed in vitro assays and in silico modeling surprisingly revealed that both hypotheses are wrong; instead, we found a more regular PA in heterogeneously deacetylated chitosans, with acetylated units overrepresented at every third position in the polymer chain. Compared to random-PA chitosans produced by homogeneous deacetylation of chitin or chemical N-acetylation of polyglucosamine, this regular PA increases the elicitation activity in plants, and generates different product profiles and distributions after enzymatic and chemical cleavage. A regular PA may be beneficial for some applications but detrimental for others, stressing the relevance of the production process for product development.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Chitosans are promising biopolymers for diverse applications, with material properties and bioactivities depending i.a. on their pattern of acetylation (PA). Commercial chitosans are typically produced by heterogeneous deacetylation of chitin, but whether this process yields chitosans with a random or block-wise PA has been debated for decades. Using a combination of recently developed in vitro assays and in silico modeling surprisingly revealed that both hypotheses are wrong; instead, we found a more regular PA in heterogeneously deacetylated chitosans, with acetylated units overrepresented at every third position in the polymer chain. Compared to random-PA chitosans produced by homogeneous deacetylation of chitin or chemical N-acetylation of polyglucosamine, this regular PA increases the elicitation activity in plants, and generates different product profiles and distributions after enzymatic and chemical cleavage. A regular PA may be beneficial for some applications but detrimental for others, stressing the relevance of the production process for product development.
Trijp, Jacobus P.; Hribernik, Nives; Lim, Jia Hui; Colle, Marlene C. S. Dal; Mena, Yadiel Vázquez; Ogawa, Yu; Delbianco, Martina
Enzyme-triggered assembly of glycan nanomaterials Journal Article
In: Angewandte Chemie International Edition, vol. n/a, no. n/a, pp. e202410634, 2024.
@article{https://doi.org/10.1002/anie.202410634b,
title = {Enzyme-triggered assembly of glycan nanomaterials},
author = {Jacobus P. Trijp and Nives Hribernik and Jia Hui Lim and Marlene C. S. Dal Colle and Yadiel Vázquez Mena and Yu Ogawa and Martina Delbianco},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.202410634},
doi = {https://doi.org/10.1002/anie.202410634},
year = {2024},
date = {2024-07-15},
journal = {Angewandte Chemie International Edition},
volume = {n/a},
number = {n/a},
pages = {e202410634},
abstract = {A comprehensive molecular understanding of carbohydrate aggregation is key to optimize carbohydrate utilization and to engineer bioinspired analogues with tailored shape1s and properties. However, the lack of well-defined synthetic standards has substantially hampered advances in this field. Herein, we employ a phosphorylation-assisted strategy to synthesize previously inaccessible long oligomers of cellulose, chitin, and xylan. These oligomers were subjected to enzyme-triggered assembly (ETA) for the on-demand formation of well-defined carbohydrate nanomaterials, including elongated platelets, helical bundles, and hexagonal particles. Cryo-electron microscopy and electron diffraction analysis provided molecular insights into the aggregation behavior of these oligosaccharides, establishing a direct connection between the resulting morphologies and the oligosaccharide primary sequence. Our findings demonstrate that ETA is a powerful approach to elucidate the intrinsic aggregation behavior of carbohydrates in nature. Moreover, the ability to access a diverse array of morphologies, expanded with a non-natural sequence, underscores the potential of ETA, coupled with sequence design, as a robust tool for accessing programmable glycan architectures.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
A comprehensive molecular understanding of carbohydrate aggregation is key to optimize carbohydrate utilization and to engineer bioinspired analogues with tailored shape1s and properties. However, the lack of well-defined synthetic standards has substantially hampered advances in this field. Herein, we employ a phosphorylation-assisted strategy to synthesize previously inaccessible long oligomers of cellulose, chitin, and xylan. These oligomers were subjected to enzyme-triggered assembly (ETA) for the on-demand formation of well-defined carbohydrate nanomaterials, including elongated platelets, helical bundles, and hexagonal particles. Cryo-electron microscopy and electron diffraction analysis provided molecular insights into the aggregation behavior of these oligosaccharides, establishing a direct connection between the resulting morphologies and the oligosaccharide primary sequence. Our findings demonstrate that ETA is a powerful approach to elucidate the intrinsic aggregation behavior of carbohydrates in nature. Moreover, the ability to access a diverse array of morphologies, expanded with a non-natural sequence, underscores the potential of ETA, coupled with sequence design, as a robust tool for accessing programmable glycan architectures.
Hellmann, Margareta J; Moerschbacher, Bruno M; Cord-Landwehr, Stefan
Fast insights into chitosan-cleaving enzymes by simultaneous analysis of polymers and oligomers through size exclusion chromatography Journal Article
In: Sci Rep, vol. 14, no. 1, pp. 3417, 2024, ISSN: 2045-2322.
@article{pmid38341520,
title = {Fast insights into chitosan-cleaving enzymes by simultaneous analysis of polymers and oligomers through size exclusion chromatography},
author = {Margareta J Hellmann and Bruno M Moerschbacher and Stefan Cord-Landwehr},
doi = {10.1038/s41598-024-54002-2},
issn = {2045-2322},
year = {2024},
date = {2024-02-01},
journal = {Sci Rep},
volume = {14},
number = {1},
pages = {3417},
abstract = {The thorough characterization of chitosan-cleaving enzymes is crucial to unveil structure-function relationships of this promising class of biomolecules for both, enzymatic fingerprinting analyses and to use the enzymes as biotechnological tools to produce tailor-made chitosans for diverse applications. Analyzing polymeric substrates as well as oligomeric products has been established as an effective way to understand the actions of enzymes, but it currently requires separate, rather laborious methods to obtain the full picture. Here, we present ultra high performance size exclusion chromatography coupled to refractive index and mass spectrometry detection (UHPSEC-RI-MS) as a straightforward method for the semi-quantitative analysis of chitosan oligomers of up to ten monomers in length. Additionally, the method allows to determine the average molecular weight of the remaining polymers and its distribution. By sampling live from an ongoing enzymatic reaction, UHPSEC-RI-MS offers the unique opportunity to analyze polymers and oligomers simultaneously-i.e., to monitor the molecular weight reduction of the polymeric substrate over the course of the digestion, while at the same time analyzing the emerging oligomeric products in a semi-quantitative manner. In this way, a single simple analysis yields detailed insights into an enzyme's action on a given substrate.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
The thorough characterization of chitosan-cleaving enzymes is crucial to unveil structure-function relationships of this promising class of biomolecules for both, enzymatic fingerprinting analyses and to use the enzymes as biotechnological tools to produce tailor-made chitosans for diverse applications. Analyzing polymeric substrates as well as oligomeric products has been established as an effective way to understand the actions of enzymes, but it currently requires separate, rather laborious methods to obtain the full picture. Here, we present ultra high performance size exclusion chromatography coupled to refractive index and mass spectrometry detection (UHPSEC-RI-MS) as a straightforward method for the semi-quantitative analysis of chitosan oligomers of up to ten monomers in length. Additionally, the method allows to determine the average molecular weight of the remaining polymers and its distribution. By sampling live from an ongoing enzymatic reaction, UHPSEC-RI-MS offers the unique opportunity to analyze polymers and oligomers simultaneously-i.e., to monitor the molecular weight reduction of the polymeric substrate over the course of the digestion, while at the same time analyzing the emerging oligomeric products in a semi-quantitative manner. In this way, a single simple analysis yields detailed insights into an enzyme's action on a given substrate.
Yu, A.; Beck, M.; Merzendorfer, H.; Yang, Q.
Advances in understanding insect chitin biosynthesis Journal Article
In: Insect Biochem Mol Biol, vol. 164, pp. 104058, 2024, ISSN: 1879-0240 (Electronic) 0965-1748 (Linking).
@article{RN7,
title = {Advances in understanding insect chitin biosynthesis},
author = {A. Yu and M. Beck and H. Merzendorfer and Q. Yang},
url = {https://www.ncbi.nlm.nih.gov/pubmed/38072083},
doi = {10.1016/j.ibmb.2023.104058},
issn = {1879-0240 (Electronic)
0965-1748 (Linking)},
year = {2024},
date = {2024-01-01},
journal = {Insect Biochem Mol Biol},
volume = {164},
pages = {104058},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Rabadiya, Dhyeykumar; Behr, Matthias
The biology of insect chitinases and their roles at chitinous cuticles Journal Article
In: Insect Biochemistry and Molecular Biology, vol. 165, pp. 104071, 2024, ISSN: 0965-1748.
@article{RABADIYA2024104071,
title = {The biology of insect chitinases and their roles at chitinous cuticles},
author = {Dhyeykumar Rabadiya and Matthias Behr},
url = {https://www.sciencedirect.com/science/article/pii/S096517482400002X},
doi = {https://doi.org/10.1016/j.ibmb.2024.104071},
issn = {0965-1748},
year = {2024},
date = {2024-01-01},
journal = {Insect Biochemistry and Molecular Biology},
volume = {165},
pages = {104071},
abstract = {Chitin is one of the most prevalent biomaterials in the natural world. The chitin matrix formation and turnover involve several enzymes for chitin synthesis, maturation, and degradation. Sequencing of the Drosophila genome more than twenty years ago revealed that insect genomes contain a number of chitinases, but why insects need so many different chitinases was unclear. Here, we focus on insect GH18 family chitinases and discuss their participation in chitin matrix formation and degradation. We describe their variations in terms of temporal and spatial expression patterns, molecular function, and physiological consequences at chitinous cuticles. We further provide insight into the catalytic mechanisms by discussing chitinase protein domain structures, substrate binding, and enzymatic activities with respect to structural analysis of the enzymatic GH18 domain, substrate-binding cleft, and characteristic TIM-barrel structure.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Chitin is one of the most prevalent biomaterials in the natural world. The chitin matrix formation and turnover involve several enzymes for chitin synthesis, maturation, and degradation. Sequencing of the Drosophila genome more than twenty years ago revealed that insect genomes contain a number of chitinases, but why insects need so many different chitinases was unclear. Here, we focus on insect GH18 family chitinases and discuss their participation in chitin matrix formation and degradation. We describe their variations in terms of temporal and spatial expression patterns, molecular function, and physiological consequences at chitinous cuticles. We further provide insight into the catalytic mechanisms by discussing chitinase protein domain structures, substrate binding, and enzymatic activities with respect to structural analysis of the enzymatic GH18 domain, substrate-binding cleft, and characteristic TIM-barrel structure.
Urca, Tomer; Lehmann, Fritz-Olaf; Gorb, Elena V.; Gorb, Stanislav N.
Nanoscale mesh acts as anti-adhesive surface against particulate contamination in eyes of whiteflies Journal Article
In: Scientific Reports, vol. 14, 2024.
@article{Urca2024NanoscaleMA,
title = {Nanoscale mesh acts as anti-adhesive surface against particulate contamination in eyes of whiteflies},
author = {Tomer Urca and Fritz-Olaf Lehmann and Elena V. Gorb and Stanislav N. Gorb},
url = {https://api.semanticscholar.org/CorpusID:271743699},
year = {2024},
date = {2024-01-01},
journal = {Scientific Reports},
volume = {14},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Lehmann, Fritz-Olaf; Gorb, Stanislav; Moussian, Bernard
In: Insect Biochemistry and Molecular Biology, vol. 168, pp. 104089, 2024, ISSN: 0965-1748.
@article{LEHMANN2024104089,
title = {Spatio-temporal distribution and genetic background of elastic proteins inside the chitin/chitosan matrix of insects including their functional significance for locomotion},
author = {Fritz-Olaf Lehmann and Stanislav Gorb and Bernard Moussian},
url = {https://www.sciencedirect.com/science/article/pii/S0965174824000201},
doi = {https://doi.org/10.1016/j.ibmb.2024.104089},
issn = {0965-1748},
year = {2024},
date = {2024-01-01},
journal = {Insect Biochemistry and Molecular Biology},
volume = {168},
pages = {104089},
abstract = {In insects, cuticle proteins interact with chitin and chitosan of the exoskeleton forming crystalline, amorphic or composite material structures. The biochemical and mechanical composition of the structure defines the cuticle's physical properties and thus how the insect cuticle behaves under mechanical stress. The tissue-specific ratio between chitin and chitosan and its pattern of deacetylation are recognized and interpreted by cuticle proteins depending on their local position in the body. Despite previous research, the assembly of the cuticle composites in time and space including its functional impact is widely unexplored. This review is devoted to the genetics underlying the temporal and spatial distribution of elastic proteins and the potential function of elastic proteins in insects with a focus on Resilin in the fruit fly Drosophila. The potential impact and function of localized patches of elastic proteins is discussed for movements in leg joints, locomotion and damage resistance of the cuticle. We conclude that an interdisciplinary research approach serves as an integral example for the molecular mechanisms of generation and interpretation of the chitin/chitosan matrix, not only in Drosophila but also in other arthropod species, and might help to synthesize artificial material composites.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
In insects, cuticle proteins interact with chitin and chitosan of the exoskeleton forming crystalline, amorphic or composite material structures. The biochemical and mechanical composition of the structure defines the cuticle's physical properties and thus how the insect cuticle behaves under mechanical stress. The tissue-specific ratio between chitin and chitosan and its pattern of deacetylation are recognized and interpreted by cuticle proteins depending on their local position in the body. Despite previous research, the assembly of the cuticle composites in time and space including its functional impact is widely unexplored. This review is devoted to the genetics underlying the temporal and spatial distribution of elastic proteins and the potential function of elastic proteins in insects with a focus on Resilin in the fruit fly Drosophila. The potential impact and function of localized patches of elastic proteins is discussed for movements in leg joints, locomotion and damage resistance of the cuticle. We conclude that an interdisciplinary research approach serves as an integral example for the molecular mechanisms of generation and interpretation of the chitin/chitosan matrix, not only in Drosophila but also in other arthropod species, and might help to synthesize artificial material composites.
2023
Anggara, K.; Srsan, L.; Jaroentomeechai, T.; Wu, X.; Rauschenbach, S.; Narimatsu, Y.; Clausen, H.; Ziegler, T.; Miller, R. L.; Kern, K.
Direct observation of glycans bonded to proteins and lipids at the single-molecule level Journal Article
In: Science, vol. 382, iss. 6667, pp. 219-223, 2023.
@article{nokey,
title = {Direct observation of glycans bonded to proteins and lipids at the single-molecule level},
author = {K. Anggara and L. Srsan and T. Jaroentomeechai and X. Wu and S. Rauschenbach and Y. Narimatsu and H. Clausen and T. Ziegler and R. L. Miller and K. Kern },
doi = {10.1126/science.adh3856},
year = {2023},
date = {2023-10-12},
urldate = {2023-10-12},
journal = {Science},
volume = {382},
issue = {6667},
pages = {219-223},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Drees, Leonard; Schneider, Susi; Riedel, Dietmar; Schuh, Reinhard; Behr, Matthias
The proteolysis of ZP proteins is essential to control cell membrane structure and integrity of developing tracheal tubes in textitDrosophila Journal Article
In: eLife, vol. 12, pp. e91079, 2023, ISSN: 2050-084X.
@article{10.7554/eLife.91079,
title = {The proteolysis of ZP proteins is essential to control cell membrane structure and integrity of developing tracheal tubes in textitDrosophila},
author = {Leonard Drees and Susi Schneider and Dietmar Riedel and Reinhard Schuh and Matthias Behr},
editor = {Elisabeth Knust and Claude Desplan},
url = {https://doi.org/10.7554/eLife.91079},
doi = {10.7554/eLife.91079},
issn = {2050-084X},
year = {2023},
date = {2023-10-01},
urldate = {2023-10-01},
journal = {eLife},
volume = {12},
pages = {e91079},
publisher = {eLife Sciences Publications, Ltd},
abstract = {Membrane expansion integrates multiple forces to mediate precise tube growth and network formation. Defects lead to deformations, as found in diseases such as polycystic kidney diseases, aortic aneurysms, stenosis, and tortuosity. We identified a mechanism of sensing and responding to the membrane-driven expansion of tracheal tubes. The apical membrane is anchored to the apical extracellular matrix (aECM) and causes expansion forces that elongate the tracheal tubes. The aECM provides a mechanical tension that balances the resulting expansion forces, with Dumpy being an elastic molecule that modulates the mechanical stress on the matrix during tracheal tube expansion. We show in textitDrosophila that the zona pellucida (ZP) domain protein Piopio interacts and cooperates with the ZP protein Dumpy at tracheal cells. To resist shear stresses which arise during tube expansion, Piopio undergoes ectodomain shedding by the Matriptase homolog Notopleural, which releases Piopio-Dumpy-mediated linkages between membranes and extracellular matrix. Failure of this process leads to deformations of the apical membrane, tears the apical matrix, and impairs tubular network function. We also show conserved ectodomain shedding of the human TGFβ type III receptor by Notopleural and the human Matriptase, providing novel findings for in-depth analysis of diseases caused by cell and tube shape changes.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Membrane expansion integrates multiple forces to mediate precise tube growth and network formation. Defects lead to deformations, as found in diseases such as polycystic kidney diseases, aortic aneurysms, stenosis, and tortuosity. We identified a mechanism of sensing and responding to the membrane-driven expansion of tracheal tubes. The apical membrane is anchored to the apical extracellular matrix (aECM) and causes expansion forces that elongate the tracheal tubes. The aECM provides a mechanical tension that balances the resulting expansion forces, with Dumpy being an elastic molecule that modulates the mechanical stress on the matrix during tracheal tube expansion. We show in textitDrosophila that the zona pellucida (ZP) domain protein Piopio interacts and cooperates with the ZP protein Dumpy at tracheal cells. To resist shear stresses which arise during tube expansion, Piopio undergoes ectodomain shedding by the Matriptase homolog Notopleural, which releases Piopio-Dumpy-mediated linkages between membranes and extracellular matrix. Failure of this process leads to deformations of the apical membrane, tears the apical matrix, and impairs tubular network function. We also show conserved ectodomain shedding of the human TGFβ type III receptor by Notopleural and the human Matriptase, providing novel findings for in-depth analysis of diseases caused by cell and tube shape changes.
Colle, Marlene C S Dal; Ricardo, Manuel G; Hribernik, Nives; Danglad-Flores, José; Seeberger, Peter H; Delbianco, Martina
Linker, loading, and reaction scale influence automated glycan assembly Journal Article
In: Beilstein J. Org. Chem., vol. 19, pp. 1015–1020, 2023, ISSN: 1860-5397.
@article{DalColle2023,
title = {Linker, loading, and reaction scale influence automated glycan assembly},
author = {Marlene C S Dal Colle and Manuel G Ricardo and Nives Hribernik and José Danglad-Flores and Peter H Seeberger and Martina Delbianco},
doi = {10.3762/bjoc.19.77},
issn = {1860-5397},
year = {2023},
date = {2023-07-06},
journal = {Beilstein J. Org. Chem.},
volume = {19},
pages = {1015--1020},
publisher = {Beilstein Institut},
abstract = {Automated glycan assembly (AGA) affords collections of well-defined glycans in a short amount of time. We systematically analyzed how parameters connected to the solid support affect the AGA outcome for three different glycan sequences. We showed that, while loading and reaction scale did not significantly influence the AGA outcome, the chemical nature of the linker dramatically altered the isolated yields. We identified that the major determinants of AGA yields are cleavage from the solid support and post-AGA purification steps. },
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Böhringer, A. C.; Deters, L.; Windfelder, A. G.; Merzendorfer, H.
Dextran sulfate sodium and uracil induce inflammatory effects and disrupt the chitinous peritrophic matrix in the midgut of Tribolium castaneum Journal Article
In: Insect Biochem Mol Biol, vol. 163, pp. 104029, 2023, ISSN: 1879-0240 (Electronic) 0965-1748 (Linking).
@article{RN14428,
title = {Dextran sulfate sodium and uracil induce inflammatory effects and disrupt the chitinous peritrophic matrix in the midgut of Tribolium castaneum},
author = {A. C. Böhringer and L. Deters and A. G. Windfelder and H. Merzendorfer},
url = {https://www.ncbi.nlm.nih.gov/pubmed/37907139},
doi = {10.1016/j.ibmb.2023.104029},
issn = {1879-0240 (Electronic)
0965-1748 (Linking)},
year = {2023},
date = {2023-01-01},
journal = {Insect Biochem Mol Biol},
volume = {163},
pages = {104029},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Rehman, H. U.; Cord-Landwehr, S.; Shapaval, V.; Dzurendova, S.; Kohler, A.; Moerschbacher, B. M.; Zimmermann, B.
High-throughput vibrational spectroscopy methods for determination of degree of acetylation for chitin and chitosan Journal Article
In: Carbohydr Polym, vol. 302, pp. 120428, 2023, ISSN: 1879-1344 (Electronic) 0144-8617 (Linking).
@article{RN5,
title = {High-throughput vibrational spectroscopy methods for determination of degree of acetylation for chitin and chitosan},
author = {H. U. Rehman and S. Cord-Landwehr and V. Shapaval and S. Dzurendova and A. Kohler and B. M. Moerschbacher and B. Zimmermann},
url = {https://www.ncbi.nlm.nih.gov/pubmed/36604090},
doi = {10.1016/j.carbpol.2022.120428},
issn = {1879-1344 (Electronic)
0144-8617 (Linking)},
year = {2023},
date = {2023-01-01},
journal = {Carbohydr Polym},
volume = {302},
pages = {120428},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Singh, R.; Smiatek, J.; Moerschbacher, B. M.
Unraveling the Impact of Acetylation Patterns in Chitosan Oligomers on Cu(2+) Ion Binding: Insights from DFT Calculations Journal Article
In: Int J Mol Sci, vol. 24, no. 18, 2023, ISSN: 1422-0067 (Electronic) 1422-0067 (Linking).
@article{RN4,
title = {Unraveling the Impact of Acetylation Patterns in Chitosan Oligomers on Cu(2+) Ion Binding: Insights from DFT Calculations},
author = {R. Singh and J. Smiatek and B. M. Moerschbacher},
url = {https://www.ncbi.nlm.nih.gov/pubmed/37762095},
doi = {10.3390/ijms241813792},
issn = {1422-0067 (Electronic)
1422-0067 (Linking)},
year = {2023},
date = {2023-01-01},
journal = {Int J Mol Sci},
volume = {24},
number = {18},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Urs, M. J.; Moerschbacher, B. M.; Cord-Landwehr, S.
Quantitative enzymatic-mass spectrometric analysis of the chitinous polymers in fungal cell walls Journal Article
In: Carbohydr Polym, vol. 301, no. Pt A, pp. 120304, 2023, ISSN: 1879-1344 (Electronic) 0144-8617 (Linking).
@article{RN6,
title = {Quantitative enzymatic-mass spectrometric analysis of the chitinous polymers in fungal cell walls},
author = {M. J. Urs and B. M. Moerschbacher and S. Cord-Landwehr},
url = {https://www.ncbi.nlm.nih.gov/pubmed/36436867},
doi = {10.1016/j.carbpol.2022.120304},
issn = {1879-1344 (Electronic)
0144-8617 (Linking)},
year = {2023},
date = {2023-01-01},
journal = {Carbohydr Polym},
volume = {301},
number = {Pt A},
pages = {120304},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
2022
Sreekumar, S.; Wattjes, J.; Niehues, A.; Mengoni, T.; Mendes, A. C.; Morris, E. R.; Goycoolea, F. M.; Moerschbacher, B. M.
Biotechnologically produced chitosans with nonrandom acetylation patterns differ from conventional chitosans in properties and activities Journal Article
In: Nat Commun, vol. 13, no. 1, pp. 7125, 2022, ISSN: 2041-1723.
@article{RN14341,
title = {Biotechnologically produced chitosans with nonrandom acetylation patterns differ from conventional chitosans in properties and activities},
author = {S. Sreekumar and J. Wattjes and A. Niehues and T. Mengoni and A. C. Mendes and E. R. Morris and F. M. Goycoolea and B. M. Moerschbacher},
doi = {10.1038/s41467-022-34483-3},
issn = {2041-1723},
year = {2022},
date = {2022-12-01},
urldate = {2022-01-01},
journal = {Nat Commun},
volume = {13},
number = {1},
pages = {7125},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Fittolani, G.; Vargová, D.; Seeberger, P. H.; Ogawa, Y.; Delbianco, M.
Bottom-Up Approach to Understand Chirality Transfer across Scales in Cellulose Assemblies Journal Article
In: J Am Chem Soc, vol. 144, no. 27, pp. 12469-12475, 2022, ISSN: 0002-7863 (Print) 0002-7863.
@article{RN14164,
title = {Bottom-Up Approach to Understand Chirality Transfer across Scales in Cellulose Assemblies},
author = {G. Fittolani and D. Vargová and P. H. Seeberger and Y. Ogawa and M. Delbianco},
doi = {10.1021/jacs.2c04522},
issn = {0002-7863 (Print) 0002-7863},
year = {2022},
date = {2022-10-01},
urldate = {2022-01-01},
journal = {J Am Chem Soc},
volume = {144},
number = {27},
pages = {12469-12475},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Chen, Wei; Cao, Peng; Liu, Yuansheng; Yu, Ailing; Wang, Dong; Chen, Lei; Sundarraj, Rajamanikandan; Yuchi, Zhiguang; Gong, Yong; Merzendorfer, Hans; Yang, Qing
Structural basis for directional chitin biosynthesis Journal Article
In: Nature, vol. 610, no. 7931, pp. 402-408, 2022, ISSN: 1476-4687.
@article{RN14239,
title = {Structural basis for directional chitin biosynthesis},
author = {Wei Chen and Peng Cao and Yuansheng Liu and Ailing Yu and Dong Wang and Lei Chen and Rajamanikandan Sundarraj and Zhiguang Yuchi and Yong Gong and Hans Merzendorfer and Qing Yang},
url = {https://doi.org/10.1038/s41586-022-05244-5},
doi = {10.1038/s41586-022-05244-5},
issn = {1476-4687},
year = {2022},
date = {2022-10-01},
urldate = {2022-01-01},
journal = {Nature},
volume = {610},
number = {7931},
pages = {402-408},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Duan, Y.; Zhu, W.; Zhao, X.; Merzendorfer, H.; Chen, J.; Zou, X.; Yang, Q.
Choline transporter-like protein 2 interacts with chitin synthase 1 and is involved in insect cuticle development Journal Article
In: Insect Biochem Mol Biol, vol. 141, pp. 103718, 2022, ISSN: 0965-1748.
@article{RN14056,
title = {Choline transporter-like protein 2 interacts with chitin synthase 1 and is involved in insect cuticle development},
author = {Y. Duan and W. Zhu and X. Zhao and H. Merzendorfer and J. Chen and X. Zou and Q. Yang},
doi = {10.1016/j.ibmb.2021.103718},
issn = {0965-1748},
year = {2022},
date = {2022-01-01},
journal = {Insect Biochem Mol Biol},
volume = {141},
pages = {103718},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Kottaipalayam-Somasundaram, S. R.; Jacob, J. P.; Aiyar, B.; Merzendorfer, H.; Nambiar-Veetil, M.
Chitin metabolism as a potential target for RNAi-based control of the forestry pest Hyblaea puera Cramer (Lepidoptera: Hyblaeidae) Journal Article
In: Pest Manag Sci, vol. 78, no. 1, pp. 296-303, 2022, ISSN: 1526-498x.
@article{RN14057,
title = {Chitin metabolism as a potential target for RNAi-based control of the forestry pest Hyblaea puera Cramer (Lepidoptera: Hyblaeidae)},
author = {S. R. Kottaipalayam-Somasundaram and J. P. Jacob and B. Aiyar and H. Merzendorfer and M. Nambiar-Veetil},
doi = {10.1002/ps.6634},
issn = {1526-498x},
year = {2022},
date = {2022-01-01},
journal = {Pest Manag Sci},
volume = {78},
number = {1},
pages = {296-303},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Zhu, W.; Duan, Y.; Chen, J.; Merzendorfer, H.; Zou, X.; Yang, Q.
SERCA interacts with chitin synthase and participates in cuticular chitin biogenesis in Drosophila Journal Article
In: Insect Biochem Mol Biol, vol. 145, pp. 103783, 2022, ISSN: 0965-1748.
@article{RN14055,
title = {SERCA interacts with chitin synthase and participates in cuticular chitin biogenesis in Drosophila},
author = {W. Zhu and Y. Duan and J. Chen and H. Merzendorfer and X. Zou and Q. Yang},
doi = {10.1016/j.ibmb.2022.103783},
issn = {0965-1748},
year = {2022},
date = {2022-01-01},
journal = {Insect Biochem Mol Biol},
volume = {145},
pages = {103783},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Lemke, P.; Jünemann, L.; Moerschbacher, B. M.
Synergistic Antimicrobial Activities of Chitosan Mixtures and Chitosan-Copper Combinations Journal Article
In: Int J Mol Sci, vol. 23, no. 6, 2022, ISSN: 1422-0067.
@article{RN14084,
title = {Synergistic Antimicrobial Activities of Chitosan Mixtures and Chitosan-Copper Combinations},
author = {P. Lemke and L. Jünemann and B. M. Moerschbacher},
doi = {10.3390/ijms23063345},
issn = {1422-0067},
year = {2022},
date = {2022-01-01},
journal = {Int J Mol Sci},
volume = {23},
number = {6},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Schröder, P.; Wattjes, J.; Schönhoff, M.; Moerschbacher, B. M.; Cramer, C.; Cord-Landwehr, S.
Quantification of chitosan in aqueous solutions by enzymatic hydrolysis and oligomer analysis via HPLC-ELSD Journal Article
In: Carbohydr Polym, vol. 283, pp. 119141, 2022, ISSN: 0144-8617.
@article{RN14085,
title = {Quantification of chitosan in aqueous solutions by enzymatic hydrolysis and oligomer analysis via HPLC-ELSD},
author = {P. Schröder and J. Wattjes and M. Schönhoff and B. M. Moerschbacher and C. Cramer and S. Cord-Landwehr},
doi = {10.1016/j.carbpol.2022.119141},
issn = {0144-8617},
year = {2022},
date = {2022-01-01},
journal = {Carbohydr Polym},
volume = {283},
pages = {119141},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Tyrikos-Ergas, T.; Gim, S.; Huang, J. Y.; Martín, S. Pinzón; Silva, D. Varón; Seeberger, P. H.; Delbianco, M.
Synthetic phosphoethanolamine-modified oligosaccharides reveal the importance of glycan length and substitution in biofilm-inspired assemblies Journal Article
In: Nat Commun, vol. 13, no. 1, pp. 3954, 2022, ISSN: 2041-1723.
@article{RN14163,
title = {Synthetic phosphoethanolamine-modified oligosaccharides reveal the importance of glycan length and substitution in biofilm-inspired assemblies},
author = {T. Tyrikos-Ergas and S. Gim and J. Y. Huang and S. Pinzón Martín and D. Varón Silva and P. H. Seeberger and M. Delbianco},
doi = {10.1038/s41467-022-31633-5},
issn = {2041-1723},
year = {2022},
date = {2022-01-01},
journal = {Nat Commun},
volume = {13},
number = {1},
pages = {3954},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Flaven-Pouchon, J.; Moussian, B.
Fluorescent Microscopy-Based Detection of Chitin in Intact Drosophila melanogaster Journal Article
In: Front Physiol, vol. 13, pp. 856369, 2022, ISSN: 1664-042X (Print) 1664-042x.
@article{RN14173,
title = {Fluorescent Microscopy-Based Detection of Chitin in Intact Drosophila melanogaster},
author = {J. Flaven-Pouchon and B. Moussian},
doi = {10.3389/fphys.2022.856369},
issn = {1664-042X (Print)
1664-042x},
year = {2022},
date = {2022-01-01},
journal = {Front Physiol},
volume = {13},
pages = {856369},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Lu, J. B.; Guo, J. S.; Chen, X.; Cheng, C.; Luo, X. M.; Zhang, X. Y.; Moussian, B.; Chen, J. P.; Li, J. M.; Zhang, C. X.
In: Insect Sci, vol. 29, no. 2, pp. 363-378, 2022, ISSN: 1672-9609.
@article{RN14175,
title = {Chitin synthase 1 and five cuticle protein genes are involved in serosal cuticle formation during early embryogenesis to enhance eggshells in Nilaparvata lugens},
author = {J. B. Lu and J. S. Guo and X. Chen and C. Cheng and X. M. Luo and X. Y. Zhang and B. Moussian and J. P. Chen and J. M. Li and C. X. Zhang},
doi = {10.1111/1744-7917.12937},
issn = {1672-9609},
year = {2022},
date = {2022-01-01},
journal = {Insect Sci},
volume = {29},
number = {2},
pages = {363-378},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Yu, R. R.; Zhang, R.; Liu, W. M.; Zhao, X. M.; Zhu, K. Y.; Moussian, B.; Zhang, J. Z.
In: Insect Mol Biol, vol. 31, no. 2, pp. 127-138, 2022, ISSN: 0962-1075.
@article{RN14174,
title = {The DOMON domain protein LmKnk contributes to correct chitin content, pore canal formation and lipid deposition in the cuticle of Locusta migratoria during moulting},
author = {R. R. Yu and R. Zhang and W. M. Liu and X. M. Zhao and K. Y. Zhu and B. Moussian and J. Z. Zhang},
doi = {10.1111/imb.12745},
issn = {0962-1075},
year = {2022},
date = {2022-01-01},
journal = {Insect Mol Biol},
volume = {31},
number = {2},
pages = {127-138},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Holzwarth, Marcel; Ludwig, Jan; Bernz, Alexander; Claasen, Birgit; Majoul, Asma; Reuter, Julia; Zens, Anna; Pawletta, Brigitte; Bilitewski, Ursula; Weiss, Ingrid M.; Laschat, Sabine
Modulating chitin synthesis in marine algae with iminosugars obtained by SmI2 and FeCl3-mediated diastereoselective carbonyl ene reaction Journal Article
In: Örg. Biomol. Chem.", vol. 20, iss. 33, pp. 6606-6618, 2022.
@article{D2OB00907B,
title = {Modulating chitin synthesis in marine algae with iminosugars obtained by SmI2 and FeCl3-mediated diastereoselective carbonyl ene reaction},
author = {Marcel Holzwarth and Jan Ludwig and Alexander Bernz and Birgit Claasen and Asma Majoul and Julia Reuter and Anna Zens and Brigitte Pawletta and Ursula Bilitewski and Ingrid M. Weiss and Sabine Laschat},
url = {http://dx.doi.org/10.1039/D2OB00907B},
doi = {10.1039/D2OB00907B},
year = {2022},
date = {2022-01-01},
journal = {Örg. Biomol. Chem."},
volume = {20},
issue = {33},
pages = {6606-6618},
publisher = {The Royal Society of Chemistry},
abstract = {Strategies for synthesizing polyhydroxylated piperidines such as iminosugars have received broad attention. These substances are known to interact with carbohydrate related enzymes, glycosidases and glycosyltransferases, to which also the large enzyme families of chitin synthases and cellulose synthases belong. Many chemical and biological aspects of chitin synthases remain unexplored due to the fact that modulating substances are hardly available or expensive. Starting from enantiopure d- and l-amino acids, a series of iminosugars was prepared by a Lewis acid-catalyzed cyclization of amino acid-derived unsaturated aldehydes as key step. Therefore, different Lewis acids were tested. For samarium diiodide we observed a superior stereoselectivity in comparison to iron(iii) chloride and methylaluminium dichloride. To increase water solubility for testing and measurement of enzyme activity, the cyclization products were further functionalized. We established a novel biological chitin synthesis test system which allows quantitative investigation of chitin synthesis in the chitin fiber producing diatom algae Thalassiosira in vivo under the light microscope. None of the compounds displayed cytotoxicity, but two of the four iminosugars increased the length of the chitin fibers produced. This is a strong indicator that these compounds mimic carbohydrates responsible for restarting chitin polymerization.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Strategies for synthesizing polyhydroxylated piperidines such as iminosugars have received broad attention. These substances are known to interact with carbohydrate related enzymes, glycosidases and glycosyltransferases, to which also the large enzyme families of chitin synthases and cellulose synthases belong. Many chemical and biological aspects of chitin synthases remain unexplored due to the fact that modulating substances are hardly available or expensive. Starting from enantiopure d- and l-amino acids, a series of iminosugars was prepared by a Lewis acid-catalyzed cyclization of amino acid-derived unsaturated aldehydes as key step. Therefore, different Lewis acids were tested. For samarium diiodide we observed a superior stereoselectivity in comparison to iron(iii) chloride and methylaluminium dichloride. To increase water solubility for testing and measurement of enzyme activity, the cyclization products were further functionalized. We established a novel biological chitin synthesis test system which allows quantitative investigation of chitin synthesis in the chitin fiber producing diatom algae Thalassiosira in vivo under the light microscope. None of the compounds displayed cytotoxicity, but two of the four iminosugars increased the length of the chitin fibers produced. This is a strong indicator that these compounds mimic carbohydrates responsible for restarting chitin polymerization.
2021
Attjioui, M.; Gillet, D.; Gueddari, N. E. El; Moerschbacher, B. M.
Synergistic Antimicrobial Effect of Chitosan Polymers and Oligomers Journal Article
In: Mol Plant Microbe Interact, vol. 34, no. 7, pp. 770-778, 2021, ISSN: 0894-0282 (Print) 0894-0282.
@article{RN14089,
title = {Synergistic Antimicrobial Effect of Chitosan Polymers and Oligomers},
author = {M. Attjioui and D. Gillet and N. E. El Gueddari and B. M. Moerschbacher},
doi = {10.1094/mpmi-07-20-0185-r},
issn = {0894-0282 (Print)
0894-0282},
year = {2021},
date = {2021-01-01},
journal = {Mol Plant Microbe Interact},
volume = {34},
number = {7},
pages = {770-778},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Bonin, M.; Hameleers, L.; Hembach, L.; Roret, T.; Cord-Landwehr, S.; Michel, G.; Moerschbacher, B. M.
In silico and in vitro analysis of an Aspergillus niger chitin deacetylase to decipher its subsite sugar preferences Journal Article
In: J Biol Chem, vol. 297, no. 4, pp. 101129, 2021, ISSN: 0021-9258 (Print) 0021-9258.
@article{RN14087,
title = {In silico and in vitro analysis of an Aspergillus niger chitin deacetylase to decipher its subsite sugar preferences},
author = {M. Bonin and L. Hameleers and L. Hembach and T. Roret and S. Cord-Landwehr and G. Michel and B. M. Moerschbacher},
doi = {10.1016/j.jbc.2021.101129},
issn = {0021-9258 (Print)
0021-9258},
year = {2021},
date = {2021-01-01},
journal = {J Biol Chem},
volume = {297},
number = {4},
pages = {101129},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Cord-Landwehr, S.; Moerschbacher, B. M.
Deciphering the ChitoCode: fungal chitins and chitosans as functional biopolymers Journal Article
In: Fungal Biol Biotechnol, vol. 8, no. 1, pp. 19, 2021, ISSN: 2054-3085.
@article{RN14086,
title = {Deciphering the ChitoCode: fungal chitins and chitosans as functional biopolymers},
author = {S. Cord-Landwehr and B. M. Moerschbacher},
doi = {10.1186/s40694-021-00127-2},
issn = {2054-3085},
year = {2021},
date = {2021-01-01},
journal = {Fungal Biol Biotechnol},
volume = {8},
number = {1},
pages = {19},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Limon, T.; Birke, A.; Monribot-Villanueva, J. L.; Guerrero-Analco, J. A.; Altúzar-Molina, A.; Carrión, G.; Goycoolea, F. M.; Moerschbacher, B. M.; Aluja, M.
In: J Sci Food Agric, vol. 101, no. 7, pp. 2756-2766, 2021, ISSN: 0022-5142.
@article{RN14092,
title = {Chitosan coatings reduce fruit fly (Anastrepha obliqua) infestation and development of the fungus Colletotrichum gloeosporioides in Manila mangoes},
author = {T. Limon and A. Birke and J. L. Monribot-Villanueva and J. A. Guerrero-Analco and A. Altúzar-Molina and G. Carrión and F. M. Goycoolea and B. M. Moerschbacher and M. Aluja},
doi = {10.1002/jsfa.10903},
issn = {0022-5142},
year = {2021},
date = {2021-01-01},
journal = {J Sci Food Agric},
volume = {101},
number = {7},
pages = {2756-2766},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Noorifar, N.; Savoian, M. S.; Ram, A.; Lukito, Y.; Hassing, B.; Weikert, T. W.; Moerschbacher, B. M.; Scott, B.
In: Mol Plant Microbe Interact, vol. 34, no. 10, pp. 1181-1192, 2021, ISSN: 0894-0282 (Print) 0894-0282.
@article{RN14088,
title = {Chitin Deacetylases Are Required for Epichloë festucae Endophytic Cell Wall Remodeling During Establishment of a Mutualistic Symbiotic Interaction with Lolium perenne},
author = {N. Noorifar and M. S. Savoian and A. Ram and Y. Lukito and B. Hassing and T. W. Weikert and B. M. Moerschbacher and B. Scott},
doi = {10.1094/mpmi-12-20-0347-r},
issn = {0894-0282 (Print)
0894-0282},
year = {2021},
date = {2021-01-01},
journal = {Mol Plant Microbe Interact},
volume = {34},
number = {10},
pages = {1181-1192},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Rizzi, Y. S.; Happel, P.; Lenz, S.; Urs, M. J.; Bonin, M.; Cord-Landwehr, S.; Singh, R.; Moerschbacher, B. M.; Kahmann, R.
Chitosan and Chitin Deacetylase Activity Are Necessary for Development and Virulence of Ustilago maydis Journal Article
In: mBio, vol. 12, no. 2, 2021.
@article{RN14090,
title = {Chitosan and Chitin Deacetylase Activity Are Necessary for Development and Virulence of Ustilago maydis},
author = {Y. S. Rizzi and P. Happel and S. Lenz and M. J. Urs and M. Bonin and S. Cord-Landwehr and R. Singh and B. M. Moerschbacher and R. Kahmann},
doi = {10.1128/mBio.03419-20},
year = {2021},
date = {2021-01-01},
journal = {mBio},
volume = {12},
number = {2},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Vortmann, M.; Stumpf, A. K.; Sgobba, E.; Dirks-Hofmeister, M. E.; Krehenbrink, M.; Wendisch, V. F.; Philipp, B.; Moerschbacher, B. M.
A bottom-up approach towards a bacterial consortium for the biotechnological conversion of chitin to L-lysine Journal Article
In: Appl Microbiol Biotechnol, vol. 105, no. 4, pp. 1547-1561, 2021, ISSN: 0175-7598 (Print) 0175-7598.
@article{RN14091,
title = {A bottom-up approach towards a bacterial consortium for the biotechnological conversion of chitin to L-lysine},
author = {M. Vortmann and A. K. Stumpf and E. Sgobba and M. E. Dirks-Hofmeister and M. Krehenbrink and V. F. Wendisch and B. Philipp and B. M. Moerschbacher},
doi = {10.1007/s00253-021-11112-5},
issn = {0175-7598 (Print)
0175-7598},
year = {2021},
date = {2021-01-01},
journal = {Appl Microbiol Biotechnol},
volume = {105},
number = {4},
pages = {1547-1561},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Politi, Y.; Bertinetti, L.; Fratzl, P.; Barth, F. G.
The spider cuticle: a remarkable material toolbox for functional diversity Journal Article
In: Philos Trans A Math Phys Eng Sci, vol. 379, no. 2206, pp. 20200332, 2021, ISSN: 1364-503X (Print) 1364-503x.
@article{RN14151,
title = {The spider cuticle: a remarkable material toolbox for functional diversity},
author = {Y. Politi and L. Bertinetti and P. Fratzl and F. G. Barth},
doi = {10.1098/rsta.2020.0332},
issn = {1364-503X (Print)
1364-503x},
year = {2021},
date = {2021-01-01},
journal = {Philos Trans A Math Phys Eng Sci},
volume = {379},
number = {2206},
pages = {20200332},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Anggara, K.; Zhu, Y.; Fittolani, G.; Yu, Y.; Tyrikos-Ergas, T.; Delbianco, M.; Rauschenbach, S.; Abb, S.; Seeberger, P. H.; Kern, K.
Identifying the origin of local flexibility in a carbohydrate polymer Journal Article
In: Proc Natl Acad Sci U S A, vol. 118, no. 23, 2021, ISSN: 0027-8424 (Print) 0027-8424.
@article{RN14159,
title = {Identifying the origin of local flexibility in a carbohydrate polymer},
author = {K. Anggara and Y. Zhu and G. Fittolani and Y. Yu and T. Tyrikos-Ergas and M. Delbianco and S. Rauschenbach and S. Abb and P. H. Seeberger and K. Kern},
doi = {10.1073/pnas.2102168118},
issn = {0027-8424 (Print)
0027-8424},
year = {2021},
date = {2021-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {118},
number = {23},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Tyrikos-Ergas, T.; Bordoni, V.; Fittolani, G.; Chaube, M. A.; Grafmüller, A.; Seeberger, P. H.; Delbianco, M.
Systematic Structural Characterization of Chitooligosaccharides Enabled by Automated Glycan Assembly Journal Article
In: Chemistry, vol. 27, no. 7, pp. 2321-2325, 2021, ISSN: 0947-6539 (Print) 0947-6539.
@article{RN14160,
title = {Systematic Structural Characterization of Chitooligosaccharides Enabled by Automated Glycan Assembly},
author = {T. Tyrikos-Ergas and V. Bordoni and G. Fittolani and M. A. Chaube and A. Grafmüller and P. H. Seeberger and M. Delbianco},
doi = {10.1002/chem.202005228},
issn = {0947-6539 (Print)
0947-6539},
year = {2021},
date = {2021-01-01},
journal = {Chemistry},
volume = {27},
number = {7},
pages = {2321-2325},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Zhu, Y.; Delbianco, M.; Seeberger, P. H.
Automated Assembly of Starch and Glycogen Polysaccharides Journal Article
In: J Am Chem Soc, vol. 143, no. 26, pp. 9758-9768, 2021, ISSN: 0002-7863 (Print) 0002-7863.
@article{RN14165,
title = {Automated Assembly of Starch and Glycogen Polysaccharides},
author = {Y. Zhu and M. Delbianco and P. H. Seeberger},
doi = {10.1021/jacs.1c02188},
issn = {0002-7863 (Print)
0002-7863},
year = {2021},
date = {2021-01-01},
journal = {J Am Chem Soc},
volume = {143},
number = {26},
pages = {9758-9768},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Zhang, M.; Ma, P. J.; Zhang, T. T.; Gao, Z. M.; Zhao, P.; Liu, X. J.; Zhang, X. Y.; Liu, W. M.; Yu, R. R.; Moussian, B.; Zhang, J. Z.
Roles of LmCDA1 and LmCDA2 in cuticle formation in the foregut and hindgut of Locusta migratoria Journal Article
In: Insect Sci, vol. 28, no. 5, pp. 1314-1325, 2021, ISSN: 1672-9609.
@article{RN14177,
title = {Roles of LmCDA1 and LmCDA2 in cuticle formation in the foregut and hindgut of Locusta migratoria},
author = {M. Zhang and P. J. Ma and T. T. Zhang and Z. M. Gao and P. Zhao and X. J. Liu and X. Y. Zhang and W. M. Liu and R. R. Yu and B. Moussian and J. Z. Zhang},
doi = {10.1111/1744-7917.12874},
issn = {1672-9609},
year = {2021},
date = {2021-01-01},
journal = {Insect Sci},
volume = {28},
number = {5},
pages = {1314-1325},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Zhang, T.; Ma, P.; Zhou, J.; He, Y.; Liu, W.; Liu, X.; Zhang, X.; Yu, R.; Zhang, M.; Moussian, B.; Zhang, J.
Group I CDAs are responsible for a selective CHC-independent cuticular barrier in Locusta migratoria Journal Article
In: Pestic Biochem Physiol, vol. 175, pp. 104854, 2021, ISSN: 0048-3575.
@article{RN14176,
title = {Group I CDAs are responsible for a selective CHC-independent cuticular barrier in Locusta migratoria},
author = {T. Zhang and P. Ma and J. Zhou and Y. He and W. Liu and X. Liu and X. Zhang and R. Yu and M. Zhang and B. Moussian and J. Zhang},
doi = {10.1016/j.pestbp.2021.104854},
issn = {0048-3575},
year = {2021},
date = {2021-01-01},
journal = {Pestic Biochem Physiol},
volume = {175},
pages = {104854},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Stegbauer, L.; Smeets, P. J. M.; Free, R.; Wallace, S. G.; Hersam, M. C.; Alp, E. E.; Joester, D.
Persistent polyamorphism in the chiton tooth: From a new biomineral to inks for additive manufacturing Journal Article
In: Proc Natl Acad Sci U S A, vol. 118, no. 23, 2021, ISSN: 0027-8424 (Print) 0027-8424.
@article{RN14217,
title = {Persistent polyamorphism in the chiton tooth: From a new biomineral to inks for additive manufacturing},
author = {L. Stegbauer and P. J. M. Smeets and R. Free and S. G. Wallace and M. C. Hersam and E. E. Alp and D. Joester},
doi = {10.1073/pnas.2020160118},
issn = {0027-8424 (Print)
0027-8424},
year = {2021},
date = {2021-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {118},
number = {23},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
2020
Rösner, J.; Wellmeyer, B.; Merzendorfer, H.
Tribolium castaneum: A Model for Investigating the Mode of Action of Insecticides and Mechanisms of Resistance Journal Article
In: Curr Pharm Des, vol. 26, no. 29, pp. 3554-3568, 2020, ISSN: 1381-6128.
@article{RN14058,
title = {Tribolium castaneum: A Model for Investigating the Mode of Action of Insecticides and Mechanisms of Resistance},
author = {J. Rösner and B. Wellmeyer and H. Merzendorfer},
doi = {10.2174/1381612826666200513113140},
issn = {1381-6128},
year = {2020},
date = {2020-01-01},
journal = {Curr Pharm Des},
volume = {26},
number = {29},
pages = {3554-3568},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Barbosa, H. F. G.; Attjioui, M.; Ferreira, A. P. G.; Moerschbacher, B. M.; É, T. G. Cavalheiro
In: Int J Biol Macromol, vol. 145, pp. 417-428, 2020, ISSN: 0141-8130.
@article{RN14099,
title = {New series of metal complexes by amphiphilic biopolymeric Schiff bases from modified chitosans: Preparation, characterization and effect of molecular weight on its biological applications},
author = {H. F. G. Barbosa and M. Attjioui and A. P. G. Ferreira and B. M. Moerschbacher and T. G. Cavalheiro É},
doi = {10.1016/j.ijbiomac.2019.12.153},
issn = {0141-8130},
year = {2020},
date = {2020-01-01},
journal = {Int J Biol Macromol},
volume = {145},
pages = {417-428},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Basa, S.; Nampally, M.; Honorato, T.; Das, S. N.; Podile, A. R.; Gueddari, N. E. El; Moerschbacher, B. M.
The Pattern of Acetylation Defines the Priming Activity of Chitosan Tetramers Journal Article
In: J Am Chem Soc, vol. 142, no. 4, pp. 1975-1986, 2020, ISSN: 0002-7863.
@article{RN14097,
title = {The Pattern of Acetylation Defines the Priming Activity of Chitosan Tetramers},
author = {S. Basa and M. Nampally and T. Honorato and S. N. Das and A. R. Podile and N. E. El Gueddari and B. M. Moerschbacher},
doi = {10.1021/jacs.9b11466},
issn = {0002-7863},
year = {2020},
date = {2020-01-01},
journal = {J Am Chem Soc},
volume = {142},
number = {4},
pages = {1975-1986},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Bonin, M.; Sreekumar, S.; Cord-Landwehr, S.; Moerschbacher, B. M.
Preparation of Defined Chitosan Oligosaccharides Using Chitin Deacetylases Journal Article
In: Int J Mol Sci, vol. 21, no. 21, 2020, ISSN: 1422-0067.
@article{RN14093,
title = {Preparation of Defined Chitosan Oligosaccharides Using Chitin Deacetylases},
author = {M. Bonin and S. Sreekumar and S. Cord-Landwehr and B. M. Moerschbacher},
doi = {10.3390/ijms21217835},
issn = {1422-0067},
year = {2020},
date = {2020-01-01},
journal = {Int J Mol Sci},
volume = {21},
number = {21},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Hembach, L.; Bonin, M.; Gorzelanny, C.; Moerschbacher, B. M.
Unique subsite specificity and potential natural function of a chitosan deacetylase from the human pathogen Cryptococcus neoformans Journal Article
In: Proc Natl Acad Sci U S A, vol. 117, no. 7, pp. 3551-3559, 2020, ISSN: 0027-8424 (Print) 0027-8424.
@article{RN14095,
title = {Unique subsite specificity and potential natural function of a chitosan deacetylase from the human pathogen Cryptococcus neoformans},
author = {L. Hembach and M. Bonin and C. Gorzelanny and B. M. Moerschbacher},
doi = {10.1073/pnas.1915798117},
issn = {0027-8424 (Print)
0027-8424},
year = {2020},
date = {2020-01-01},
journal = {Proc Natl Acad Sci U S A},
volume = {117},
number = {7},
pages = {3551-3559},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Regel, E. K.; Evers, M.; Liss, M.; Cord-Landwehr, S.; Moerschbacher, B. M.
High-Throughput Screening Using UHPLC-MS To Characterize the Subsite Specificities of Chitosanases or Chitinases Journal Article
In: Anal Chem, vol. 92, no. 4, pp. 3246-3252, 2020, ISSN: 0003-2700.
@article{RN14096,
title = {High-Throughput Screening Using UHPLC-MS To Characterize the Subsite Specificities of Chitosanases or Chitinases},
author = {E. K. Regel and M. Evers and M. Liss and S. Cord-Landwehr and B. M. Moerschbacher},
doi = {10.1021/acs.analchem.9b05049},
issn = {0003-2700},
year = {2020},
date = {2020-01-01},
journal = {Anal Chem},
volume = {92},
number = {4},
pages = {3246-3252},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Leeuwe, T. M.; Wattjes, J.; Niehues, A.; Forn-Cuní, G.; Geoffrion, N.; Mélida, H.; Arentshorst, M.; Molina, A.; Tsang, A.; Meijer, A. H.; Moerschbacher, B. M.; Punt, P. J.; Ram, A. F. J.
In: Cell Surf, vol. 6, pp. 100039, 2020, ISSN: 2468-2330.
@article{RN14094,
title = {A seven-membered cell wall related transglycosylase gene family in Aspergillus niger is relevant for cell wall integrity in cell wall mutants with reduced α-glucan or galactomannan},
author = {T. M. Leeuwe and J. Wattjes and A. Niehues and G. Forn-Cuní and N. Geoffrion and H. Mélida and M. Arentshorst and A. Molina and A. Tsang and A. H. Meijer and B. M. Moerschbacher and P. J. Punt and A. F. J. Ram},
doi = {10.1016/j.tcsw.2020.100039},
issn = {2468-2330},
year = {2020},
date = {2020-01-01},
journal = {Cell Surf},
volume = {6},
pages = {100039},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Wattjes, J.; Niehues, A.; Moerschbacher, B. M.
Robust enzymatic-mass spectrometric fingerprinting analysis of the fraction of acetylation of chitosans Journal Article
In: Carbohydr Polym, vol. 231, pp. 115684, 2020, ISSN: 0144-8617.
@article{RN14098,
title = {Robust enzymatic-mass spectrometric fingerprinting analysis of the fraction of acetylation of chitosans},
author = {J. Wattjes and A. Niehues and B. M. Moerschbacher},
doi = {10.1016/j.carbpol.2019.115684},
issn = {0144-8617},
year = {2020},
date = {2020-01-01},
journal = {Carbohydr Polym},
volume = {231},
pages = {115684},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Search for a specific publication, author or title:
Lindner, Sandra; Bonin, Martin; Hellmann, Margareta J.; Moerschbacher, Bruno M.
Three intertwining effects guide the mode of action of chitin deacetylase de- and N-acetylation reactions Journal Article
In: Carbohydrate Polymers, vol. 347, pp. 122725, 2024, ISSN: 0144-8617.
@article{LINDNER2025122725,
title = {Three intertwining effects guide the mode of action of chitin deacetylase de- and N-acetylation reactions},
author = {Sandra Lindner and Martin Bonin and Margareta J. Hellmann and Bruno M. Moerschbacher},
url = {https://www.sciencedirect.com/science/article/pii/S0144861724009512},
doi = {https://doi.org/10.1016/j.carbpol.2024.122725},
issn = {0144-8617},
year = {2024},
date = {2024-09-23},
urldate = {2025-01-01},
journal = {Carbohydrate Polymers},
volume = {347},
pages = {122725},
abstract = {Chitosans are promising multi-functional biomolecules for various applications whose performance is dependent on three key structural parameters, including the pattern of acetylation (PA). To date, chitin deacetylases (CDAs) are the only tool to control the PA of chitosan polymers via their specific mode of action during de- or N-acetylation. For a start, this review summarizes the current state of research on the classification of carbohydrate esterase 4 enzymes, the features in sequence and structure of CDAs, and the different PAs produced by different CDAs during de- or N-acetylation. In the main part, we introduce three effects that guide the mode of action of these enzymes: the already established subsite capping effect, the subsite occupation effect, and the subsite preference effect. We show how their interplay controls the PA of CDA products and describe their molecular basis. For one thing, this review aims to equip the reader with the knowledge to understand and analyze CDAs – including a guide for in silico and in vitro analyses. But more importantly, we intend to reform and extend the model explaining their mode of action on chitosans to facilitate a deeper understanding of these important enzymes for biology and biotechnology.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Chitosans are promising multi-functional biomolecules for various applications whose performance is dependent on three key structural parameters, including the pattern of acetylation (PA). To date, chitin deacetylases (CDAs) are the only tool to control the PA of chitosan polymers via their specific mode of action during de- or N-acetylation. For a start, this review summarizes the current state of research on the classification of carbohydrate esterase 4 enzymes, the features in sequence and structure of CDAs, and the different PAs produced by different CDAs during de- or N-acetylation. In the main part, we introduce three effects that guide the mode of action of these enzymes: the already established subsite capping effect, the subsite occupation effect, and the subsite preference effect. We show how their interplay controls the PA of CDA products and describe their molecular basis. For one thing, this review aims to equip the reader with the knowledge to understand and analyze CDAs – including a guide for in silico and in vitro analyses. But more importantly, we intend to reform and extend the model explaining their mode of action on chitosans to facilitate a deeper understanding of these important enzymes for biology and biotechnology.
Hellmann, Margareta J; Gillet, Dominique; Trombotto, Stéphane; Raetz, Sonja; Moerschbacher, Bruno M; Cord-Landwehr, Stefan
Heterogeneously deacetylated chitosans possess an unexpected regular pattern favoring acetylation at every third position Journal Article
In: Nat Commun, vol. 15, no. 1, pp. 6695, 2024, ISSN: 2041-1723.
@article{pmid39107282,
title = {Heterogeneously deacetylated chitosans possess an unexpected regular pattern favoring acetylation at every third position},
author = {Margareta J Hellmann and Dominique Gillet and Stéphane Trombotto and Sonja Raetz and Bruno M Moerschbacher and Stefan Cord-Landwehr},
doi = {10.1038/s41467-024-50857-1},
issn = {2041-1723},
year = {2024},
date = {2024-08-01},
journal = {Nat Commun},
volume = {15},
number = {1},
pages = {6695},
abstract = {Chitosans are promising biopolymers for diverse applications, with material properties and bioactivities depending i.a. on their pattern of acetylation (PA). Commercial chitosans are typically produced by heterogeneous deacetylation of chitin, but whether this process yields chitosans with a random or block-wise PA has been debated for decades. Using a combination of recently developed in vitro assays and in silico modeling surprisingly revealed that both hypotheses are wrong; instead, we found a more regular PA in heterogeneously deacetylated chitosans, with acetylated units overrepresented at every third position in the polymer chain. Compared to random-PA chitosans produced by homogeneous deacetylation of chitin or chemical N-acetylation of polyglucosamine, this regular PA increases the elicitation activity in plants, and generates different product profiles and distributions after enzymatic and chemical cleavage. A regular PA may be beneficial for some applications but detrimental for others, stressing the relevance of the production process for product development.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Chitosans are promising biopolymers for diverse applications, with material properties and bioactivities depending i.a. on their pattern of acetylation (PA). Commercial chitosans are typically produced by heterogeneous deacetylation of chitin, but whether this process yields chitosans with a random or block-wise PA has been debated for decades. Using a combination of recently developed in vitro assays and in silico modeling surprisingly revealed that both hypotheses are wrong; instead, we found a more regular PA in heterogeneously deacetylated chitosans, with acetylated units overrepresented at every third position in the polymer chain. Compared to random-PA chitosans produced by homogeneous deacetylation of chitin or chemical N-acetylation of polyglucosamine, this regular PA increases the elicitation activity in plants, and generates different product profiles and distributions after enzymatic and chemical cleavage. A regular PA may be beneficial for some applications but detrimental for others, stressing the relevance of the production process for product development.
Trijp, Jacobus P.; Hribernik, Nives; Lim, Jia Hui; Colle, Marlene C. S. Dal; Mena, Yadiel Vázquez; Ogawa, Yu; Delbianco, Martina
Enzyme-triggered assembly of glycan nanomaterials Journal Article
In: Angewandte Chemie International Edition, vol. n/a, no. n/a, pp. e202410634, 2024.
@article{https://doi.org/10.1002/anie.202410634b,
title = {Enzyme-triggered assembly of glycan nanomaterials},
author = {Jacobus P. Trijp and Nives Hribernik and Jia Hui Lim and Marlene C. S. Dal Colle and Yadiel Vázquez Mena and Yu Ogawa and Martina Delbianco},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.202410634},
doi = {https://doi.org/10.1002/anie.202410634},
year = {2024},
date = {2024-07-15},
journal = {Angewandte Chemie International Edition},
volume = {n/a},
number = {n/a},
pages = {e202410634},
abstract = {A comprehensive molecular understanding of carbohydrate aggregation is key to optimize carbohydrate utilization and to engineer bioinspired analogues with tailored shape1s and properties. However, the lack of well-defined synthetic standards has substantially hampered advances in this field. Herein, we employ a phosphorylation-assisted strategy to synthesize previously inaccessible long oligomers of cellulose, chitin, and xylan. These oligomers were subjected to enzyme-triggered assembly (ETA) for the on-demand formation of well-defined carbohydrate nanomaterials, including elongated platelets, helical bundles, and hexagonal particles. Cryo-electron microscopy and electron diffraction analysis provided molecular insights into the aggregation behavior of these oligosaccharides, establishing a direct connection between the resulting morphologies and the oligosaccharide primary sequence. Our findings demonstrate that ETA is a powerful approach to elucidate the intrinsic aggregation behavior of carbohydrates in nature. Moreover, the ability to access a diverse array of morphologies, expanded with a non-natural sequence, underscores the potential of ETA, coupled with sequence design, as a robust tool for accessing programmable glycan architectures.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
A comprehensive molecular understanding of carbohydrate aggregation is key to optimize carbohydrate utilization and to engineer bioinspired analogues with tailored shape1s and properties. However, the lack of well-defined synthetic standards has substantially hampered advances in this field. Herein, we employ a phosphorylation-assisted strategy to synthesize previously inaccessible long oligomers of cellulose, chitin, and xylan. These oligomers were subjected to enzyme-triggered assembly (ETA) for the on-demand formation of well-defined carbohydrate nanomaterials, including elongated platelets, helical bundles, and hexagonal particles. Cryo-electron microscopy and electron diffraction analysis provided molecular insights into the aggregation behavior of these oligosaccharides, establishing a direct connection between the resulting morphologies and the oligosaccharide primary sequence. Our findings demonstrate that ETA is a powerful approach to elucidate the intrinsic aggregation behavior of carbohydrates in nature. Moreover, the ability to access a diverse array of morphologies, expanded with a non-natural sequence, underscores the potential of ETA, coupled with sequence design, as a robust tool for accessing programmable glycan architectures.
Hellmann, Margareta J; Moerschbacher, Bruno M; Cord-Landwehr, Stefan
Fast insights into chitosan-cleaving enzymes by simultaneous analysis of polymers and oligomers through size exclusion chromatography Journal Article
In: Sci Rep, vol. 14, no. 1, pp. 3417, 2024, ISSN: 2045-2322.
@article{pmid38341520,
title = {Fast insights into chitosan-cleaving enzymes by simultaneous analysis of polymers and oligomers through size exclusion chromatography},
author = {Margareta J Hellmann and Bruno M Moerschbacher and Stefan Cord-Landwehr},
doi = {10.1038/s41598-024-54002-2},
issn = {2045-2322},
year = {2024},
date = {2024-02-01},
journal = {Sci Rep},
volume = {14},
number = {1},
pages = {3417},
abstract = {The thorough characterization of chitosan-cleaving enzymes is crucial to unveil structure-function relationships of this promising class of biomolecules for both, enzymatic fingerprinting analyses and to use the enzymes as biotechnological tools to produce tailor-made chitosans for diverse applications. Analyzing polymeric substrates as well as oligomeric products has been established as an effective way to understand the actions of enzymes, but it currently requires separate, rather laborious methods to obtain the full picture. Here, we present ultra high performance size exclusion chromatography coupled to refractive index and mass spectrometry detection (UHPSEC-RI-MS) as a straightforward method for the semi-quantitative analysis of chitosan oligomers of up to ten monomers in length. Additionally, the method allows to determine the average molecular weight of the remaining polymers and its distribution. By sampling live from an ongoing enzymatic reaction, UHPSEC-RI-MS offers the unique opportunity to analyze polymers and oligomers simultaneously-i.e., to monitor the molecular weight reduction of the polymeric substrate over the course of the digestion, while at the same time analyzing the emerging oligomeric products in a semi-quantitative manner. In this way, a single simple analysis yields detailed insights into an enzyme's action on a given substrate.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
The thorough characterization of chitosan-cleaving enzymes is crucial to unveil structure-function relationships of this promising class of biomolecules for both, enzymatic fingerprinting analyses and to use the enzymes as biotechnological tools to produce tailor-made chitosans for diverse applications. Analyzing polymeric substrates as well as oligomeric products has been established as an effective way to understand the actions of enzymes, but it currently requires separate, rather laborious methods to obtain the full picture. Here, we present ultra high performance size exclusion chromatography coupled to refractive index and mass spectrometry detection (UHPSEC-RI-MS) as a straightforward method for the semi-quantitative analysis of chitosan oligomers of up to ten monomers in length. Additionally, the method allows to determine the average molecular weight of the remaining polymers and its distribution. By sampling live from an ongoing enzymatic reaction, UHPSEC-RI-MS offers the unique opportunity to analyze polymers and oligomers simultaneously-i.e., to monitor the molecular weight reduction of the polymeric substrate over the course of the digestion, while at the same time analyzing the emerging oligomeric products in a semi-quantitative manner. In this way, a single simple analysis yields detailed insights into an enzyme's action on a given substrate.
Yu, A.; Beck, M.; Merzendorfer, H.; Yang, Q.
Advances in understanding insect chitin biosynthesis Journal Article
In: Insect Biochem Mol Biol, vol. 164, pp. 104058, 2024, ISSN: 1879-0240 (Electronic) 0965-1748 (Linking).
@article{RN7,
title = {Advances in understanding insect chitin biosynthesis},
author = {A. Yu and M. Beck and H. Merzendorfer and Q. Yang},
url = {https://www.ncbi.nlm.nih.gov/pubmed/38072083},
doi = {10.1016/j.ibmb.2023.104058},
issn = {1879-0240 (Electronic)
0965-1748 (Linking)},
year = {2024},
date = {2024-01-01},
journal = {Insect Biochem Mol Biol},
volume = {164},
pages = {104058},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Rabadiya, Dhyeykumar; Behr, Matthias
The biology of insect chitinases and their roles at chitinous cuticles Journal Article
In: Insect Biochemistry and Molecular Biology, vol. 165, pp. 104071, 2024, ISSN: 0965-1748.
@article{RABADIYA2024104071,
title = {The biology of insect chitinases and their roles at chitinous cuticles},
author = {Dhyeykumar Rabadiya and Matthias Behr},
url = {https://www.sciencedirect.com/science/article/pii/S096517482400002X},
doi = {https://doi.org/10.1016/j.ibmb.2024.104071},
issn = {0965-1748},
year = {2024},
date = {2024-01-01},
journal = {Insect Biochemistry and Molecular Biology},
volume = {165},
pages = {104071},
abstract = {Chitin is one of the most prevalent biomaterials in the natural world. The chitin matrix formation and turnover involve several enzymes for chitin synthesis, maturation, and degradation. Sequencing of the Drosophila genome more than twenty years ago revealed that insect genomes contain a number of chitinases, but why insects need so many different chitinases was unclear. Here, we focus on insect GH18 family chitinases and discuss their participation in chitin matrix formation and degradation. We describe their variations in terms of temporal and spatial expression patterns, molecular function, and physiological consequences at chitinous cuticles. We further provide insight into the catalytic mechanisms by discussing chitinase protein domain structures, substrate binding, and enzymatic activities with respect to structural analysis of the enzymatic GH18 domain, substrate-binding cleft, and characteristic TIM-barrel structure.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Chitin is one of the most prevalent biomaterials in the natural world. The chitin matrix formation and turnover involve several enzymes for chitin synthesis, maturation, and degradation. Sequencing of the Drosophila genome more than twenty years ago revealed that insect genomes contain a number of chitinases, but why insects need so many different chitinases was unclear. Here, we focus on insect GH18 family chitinases and discuss their participation in chitin matrix formation and degradation. We describe their variations in terms of temporal and spatial expression patterns, molecular function, and physiological consequences at chitinous cuticles. We further provide insight into the catalytic mechanisms by discussing chitinase protein domain structures, substrate binding, and enzymatic activities with respect to structural analysis of the enzymatic GH18 domain, substrate-binding cleft, and characteristic TIM-barrel structure.
Urca, Tomer; Lehmann, Fritz-Olaf; Gorb, Elena V.; Gorb, Stanislav N.
Nanoscale mesh acts as anti-adhesive surface against particulate contamination in eyes of whiteflies Journal Article
In: Scientific Reports, vol. 14, 2024.
@article{Urca2024NanoscaleMA,
title = {Nanoscale mesh acts as anti-adhesive surface against particulate contamination in eyes of whiteflies},
author = {Tomer Urca and Fritz-Olaf Lehmann and Elena V. Gorb and Stanislav N. Gorb},
url = {https://api.semanticscholar.org/CorpusID:271743699},
year = {2024},
date = {2024-01-01},
journal = {Scientific Reports},
volume = {14},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Lehmann, Fritz-Olaf; Gorb, Stanislav; Moussian, Bernard
In: Insect Biochemistry and Molecular Biology, vol. 168, pp. 104089, 2024, ISSN: 0965-1748.
@article{LEHMANN2024104089,
title = {Spatio-temporal distribution and genetic background of elastic proteins inside the chitin/chitosan matrix of insects including their functional significance for locomotion},
author = {Fritz-Olaf Lehmann and Stanislav Gorb and Bernard Moussian},
url = {https://www.sciencedirect.com/science/article/pii/S0965174824000201},
doi = {https://doi.org/10.1016/j.ibmb.2024.104089},
issn = {0965-1748},
year = {2024},
date = {2024-01-01},
journal = {Insect Biochemistry and Molecular Biology},
volume = {168},
pages = {104089},
abstract = {In insects, cuticle proteins interact with chitin and chitosan of the exoskeleton forming crystalline, amorphic or composite material structures. The biochemical and mechanical composition of the structure defines the cuticle's physical properties and thus how the insect cuticle behaves under mechanical stress. The tissue-specific ratio between chitin and chitosan and its pattern of deacetylation are recognized and interpreted by cuticle proteins depending on their local position in the body. Despite previous research, the assembly of the cuticle composites in time and space including its functional impact is widely unexplored. This review is devoted to the genetics underlying the temporal and spatial distribution of elastic proteins and the potential function of elastic proteins in insects with a focus on Resilin in the fruit fly Drosophila. The potential impact and function of localized patches of elastic proteins is discussed for movements in leg joints, locomotion and damage resistance of the cuticle. We conclude that an interdisciplinary research approach serves as an integral example for the molecular mechanisms of generation and interpretation of the chitin/chitosan matrix, not only in Drosophila but also in other arthropod species, and might help to synthesize artificial material composites.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
In insects, cuticle proteins interact with chitin and chitosan of the exoskeleton forming crystalline, amorphic or composite material structures. The biochemical and mechanical composition of the structure defines the cuticle's physical properties and thus how the insect cuticle behaves under mechanical stress. The tissue-specific ratio between chitin and chitosan and its pattern of deacetylation are recognized and interpreted by cuticle proteins depending on their local position in the body. Despite previous research, the assembly of the cuticle composites in time and space including its functional impact is widely unexplored. This review is devoted to the genetics underlying the temporal and spatial distribution of elastic proteins and the potential function of elastic proteins in insects with a focus on Resilin in the fruit fly Drosophila. The potential impact and function of localized patches of elastic proteins is discussed for movements in leg joints, locomotion and damage resistance of the cuticle. We conclude that an interdisciplinary research approach serves as an integral example for the molecular mechanisms of generation and interpretation of the chitin/chitosan matrix, not only in Drosophila but also in other arthropod species, and might help to synthesize artificial material composites.
Anggara, K.; Srsan, L.; Jaroentomeechai, T.; Wu, X.; Rauschenbach, S.; Narimatsu, Y.; Clausen, H.; Ziegler, T.; Miller, R. L.; Kern, K.
Direct observation of glycans bonded to proteins and lipids at the single-molecule level Journal Article
In: Science, vol. 382, iss. 6667, pp. 219-223, 2023.
@article{nokey,
title = {Direct observation of glycans bonded to proteins and lipids at the single-molecule level},
author = {K. Anggara and L. Srsan and T. Jaroentomeechai and X. Wu and S. Rauschenbach and Y. Narimatsu and H. Clausen and T. Ziegler and R. L. Miller and K. Kern },
doi = {10.1126/science.adh3856},
year = {2023},
date = {2023-10-12},
urldate = {2023-10-12},
journal = {Science},
volume = {382},
issue = {6667},
pages = {219-223},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Drees, Leonard; Schneider, Susi; Riedel, Dietmar; Schuh, Reinhard; Behr, Matthias
The proteolysis of ZP proteins is essential to control cell membrane structure and integrity of developing tracheal tubes in textitDrosophila Journal Article
In: eLife, vol. 12, pp. e91079, 2023, ISSN: 2050-084X.
@article{10.7554/eLife.91079,
title = {The proteolysis of ZP proteins is essential to control cell membrane structure and integrity of developing tracheal tubes in textitDrosophila},
author = {Leonard Drees and Susi Schneider and Dietmar Riedel and Reinhard Schuh and Matthias Behr},
editor = {Elisabeth Knust and Claude Desplan},
url = {https://doi.org/10.7554/eLife.91079},
doi = {10.7554/eLife.91079},
issn = {2050-084X},
year = {2023},
date = {2023-10-01},
urldate = {2023-10-01},
journal = {eLife},
volume = {12},
pages = {e91079},
publisher = {eLife Sciences Publications, Ltd},
abstract = {Membrane expansion integrates multiple forces to mediate precise tube growth and network formation. Defects lead to deformations, as found in diseases such as polycystic kidney diseases, aortic aneurysms, stenosis, and tortuosity. We identified a mechanism of sensing and responding to the membrane-driven expansion of tracheal tubes. The apical membrane is anchored to the apical extracellular matrix (aECM) and causes expansion forces that elongate the tracheal tubes. The aECM provides a mechanical tension that balances the resulting expansion forces, with Dumpy being an elastic molecule that modulates the mechanical stress on the matrix during tracheal tube expansion. We show in textitDrosophila that the zona pellucida (ZP) domain protein Piopio interacts and cooperates with the ZP protein Dumpy at tracheal cells. To resist shear stresses which arise during tube expansion, Piopio undergoes ectodomain shedding by the Matriptase homolog Notopleural, which releases Piopio-Dumpy-mediated linkages between membranes and extracellular matrix. Failure of this process leads to deformations of the apical membrane, tears the apical matrix, and impairs tubular network function. We also show conserved ectodomain shedding of the human TGFβ type III receptor by Notopleural and the human Matriptase, providing novel findings for in-depth analysis of diseases caused by cell and tube shape changes.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Membrane expansion integrates multiple forces to mediate precise tube growth and network formation. Defects lead to deformations, as found in diseases such as polycystic kidney diseases, aortic aneurysms, stenosis, and tortuosity. We identified a mechanism of sensing and responding to the membrane-driven expansion of tracheal tubes. The apical membrane is anchored to the apical extracellular matrix (aECM) and causes expansion forces that elongate the tracheal tubes. The aECM provides a mechanical tension that balances the resulting expansion forces, with Dumpy being an elastic molecule that modulates the mechanical stress on the matrix during tracheal tube expansion. We show in textitDrosophila that the zona pellucida (ZP) domain protein Piopio interacts and cooperates with the ZP protein Dumpy at tracheal cells. To resist shear stresses which arise during tube expansion, Piopio undergoes ectodomain shedding by the Matriptase homolog Notopleural, which releases Piopio-Dumpy-mediated linkages between membranes and extracellular matrix. Failure of this process leads to deformations of the apical membrane, tears the apical matrix, and impairs tubular network function. We also show conserved ectodomain shedding of the human TGFβ type III receptor by Notopleural and the human Matriptase, providing novel findings for in-depth analysis of diseases caused by cell and tube shape changes.
Colle, Marlene C S Dal; Ricardo, Manuel G; Hribernik, Nives; Danglad-Flores, José; Seeberger, Peter H; Delbianco, Martina
Linker, loading, and reaction scale influence automated glycan assembly Journal Article
In: Beilstein J. Org. Chem., vol. 19, pp. 1015–1020, 2023, ISSN: 1860-5397.
@article{DalColle2023,
title = {Linker, loading, and reaction scale influence automated glycan assembly},
author = {Marlene C S Dal Colle and Manuel G Ricardo and Nives Hribernik and José Danglad-Flores and Peter H Seeberger and Martina Delbianco},
doi = {10.3762/bjoc.19.77},
issn = {1860-5397},
year = {2023},
date = {2023-07-06},
journal = {Beilstein J. Org. Chem.},
volume = {19},
pages = {1015--1020},
publisher = {Beilstein Institut},
abstract = {Automated glycan assembly (AGA) affords collections of well-defined glycans in a short amount of time. We systematically analyzed how parameters connected to the solid support affect the AGA outcome for three different glycan sequences. We showed that, while loading and reaction scale did not significantly influence the AGA outcome, the chemical nature of the linker dramatically altered the isolated yields. We identified that the major determinants of AGA yields are cleavage from the solid support and post-AGA purification steps. },
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Böhringer, A. C.; Deters, L.; Windfelder, A. G.; Merzendorfer, H.
Dextran sulfate sodium and uracil induce inflammatory effects and disrupt the chitinous peritrophic matrix in the midgut of Tribolium castaneum Journal Article
In: Insect Biochem Mol Biol, vol. 163, pp. 104029, 2023, ISSN: 1879-0240 (Electronic) 0965-1748 (Linking).
@article{RN14428,
title = {Dextran sulfate sodium and uracil induce inflammatory effects and disrupt the chitinous peritrophic matrix in the midgut of Tribolium castaneum},
author = {A. C. Böhringer and L. Deters and A. G. Windfelder and H. Merzendorfer},
url = {https://www.ncbi.nlm.nih.gov/pubmed/37907139},
doi = {10.1016/j.ibmb.2023.104029},
issn = {1879-0240 (Electronic)
0965-1748 (Linking)},
year = {2023},
date = {2023-01-01},
journal = {Insect Biochem Mol Biol},
volume = {163},
pages = {104029},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Rehman, H. U.; Cord-Landwehr, S.; Shapaval, V.; Dzurendova, S.; Kohler, A.; Moerschbacher, B. M.; Zimmermann, B.
High-throughput vibrational spectroscopy methods for determination of degree of acetylation for chitin and chitosan Journal Article
In: Carbohydr Polym, vol. 302, pp. 120428, 2023, ISSN: 1879-1344 (Electronic) 0144-8617 (Linking).
@article{RN5,
title = {High-throughput vibrational spectroscopy methods for determination of degree of acetylation for chitin and chitosan},
author = {H. U. Rehman and S. Cord-Landwehr and V. Shapaval and S. Dzurendova and A. Kohler and B. M. Moerschbacher and B. Zimmermann},
url = {https://www.ncbi.nlm.nih.gov/pubmed/36604090},
doi = {10.1016/j.carbpol.2022.120428},
issn = {1879-1344 (Electronic)
0144-8617 (Linking)},
year = {2023},
date = {2023-01-01},
journal = {Carbohydr Polym},
volume = {302},
pages = {120428},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Singh, R.; Smiatek, J.; Moerschbacher, B. M.
Unraveling the Impact of Acetylation Patterns in Chitosan Oligomers on Cu(2+) Ion Binding: Insights from DFT Calculations Journal Article
In: Int J Mol Sci, vol. 24, no. 18, 2023, ISSN: 1422-0067 (Electronic) 1422-0067 (Linking).
@article{RN4,
title = {Unraveling the Impact of Acetylation Patterns in Chitosan Oligomers on Cu(2+) Ion Binding: Insights from DFT Calculations},
author = {R. Singh and J. Smiatek and B. M. Moerschbacher},
url = {https://www.ncbi.nlm.nih.gov/pubmed/37762095},
doi = {10.3390/ijms241813792},
issn = {1422-0067 (Electronic)
1422-0067 (Linking)},
year = {2023},
date = {2023-01-01},
journal = {Int J Mol Sci},
volume = {24},
number = {18},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Urs, M. J.; Moerschbacher, B. M.; Cord-Landwehr, S.
Quantitative enzymatic-mass spectrometric analysis of the chitinous polymers in fungal cell walls Journal Article
In: Carbohydr Polym, vol. 301, no. Pt A, pp. 120304, 2023, ISSN: 1879-1344 (Electronic) 0144-8617 (Linking).
@article{RN6,
title = {Quantitative enzymatic-mass spectrometric analysis of the chitinous polymers in fungal cell walls},
author = {M. J. Urs and B. M. Moerschbacher and S. Cord-Landwehr},
url = {https://www.ncbi.nlm.nih.gov/pubmed/36436867},
doi = {10.1016/j.carbpol.2022.120304},
issn = {1879-1344 (Electronic)
0144-8617 (Linking)},
year = {2023},
date = {2023-01-01},
journal = {Carbohydr Polym},
volume = {301},
number = {Pt A},
pages = {120304},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Sreekumar, S.; Wattjes, J.; Niehues, A.; Mengoni, T.; Mendes, A. C.; Morris, E. R.; Goycoolea, F. M.; Moerschbacher, B. M.
Biotechnologically produced chitosans with nonrandom acetylation patterns differ from conventional chitosans in properties and activities Journal Article
In: Nat Commun, vol. 13, no. 1, pp. 7125, 2022, ISSN: 2041-1723.
@article{RN14341,
title = {Biotechnologically produced chitosans with nonrandom acetylation patterns differ from conventional chitosans in properties and activities},
author = {S. Sreekumar and J. Wattjes and A. Niehues and T. Mengoni and A. C. Mendes and E. R. Morris and F. M. Goycoolea and B. M. Moerschbacher},
doi = {10.1038/s41467-022-34483-3},
issn = {2041-1723},
year = {2022},
date = {2022-12-01},
urldate = {2022-01-01},
journal = {Nat Commun},
volume = {13},
number = {1},
pages = {7125},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Fittolani, G.; Vargová, D.; Seeberger, P. H.; Ogawa, Y.; Delbianco, M.
Bottom-Up Approach to Understand Chirality Transfer across Scales in Cellulose Assemblies Journal Article
In: J Am Chem Soc, vol. 144, no. 27, pp. 12469-12475, 2022, ISSN: 0002-7863 (Print) 0002-7863.
@article{RN14164,
title = {Bottom-Up Approach to Understand Chirality Transfer across Scales in Cellulose Assemblies},
author = {G. Fittolani and D. Vargová and P. H. Seeberger and Y. Ogawa and M. Delbianco},
doi = {10.1021/jacs.2c04522},
issn = {0002-7863 (Print) 0002-7863},
year = {2022},
date = {2022-10-01},
urldate = {2022-01-01},
journal = {J Am Chem Soc},
volume = {144},
number = {27},
pages = {12469-12475},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Chen, Wei; Cao, Peng; Liu, Yuansheng; Yu, Ailing; Wang, Dong; Chen, Lei; Sundarraj, Rajamanikandan; Yuchi, Zhiguang; Gong, Yong; Merzendorfer, Hans; Yang, Qing
Structural basis for directional chitin biosynthesis Journal Article
In: Nature, vol. 610, no. 7931, pp. 402-408, 2022, ISSN: 1476-4687.
@article{RN14239,
title = {Structural basis for directional chitin biosynthesis},
author = {Wei Chen and Peng Cao and Yuansheng Liu and Ailing Yu and Dong Wang and Lei Chen and Rajamanikandan Sundarraj and Zhiguang Yuchi and Yong Gong and Hans Merzendorfer and Qing Yang},
url = {https://doi.org/10.1038/s41586-022-05244-5},
doi = {10.1038/s41586-022-05244-5},
issn = {1476-4687},
year = {2022},
date = {2022-10-01},
urldate = {2022-01-01},
journal = {Nature},
volume = {610},
number = {7931},
pages = {402-408},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Duan, Y.; Zhu, W.; Zhao, X.; Merzendorfer, H.; Chen, J.; Zou, X.; Yang, Q.
Choline transporter-like protein 2 interacts with chitin synthase 1 and is involved in insect cuticle development Journal Article
In: Insect Biochem Mol Biol, vol. 141, pp. 103718, 2022, ISSN: 0965-1748.
@article{RN14056,
title = {Choline transporter-like protein 2 interacts with chitin synthase 1 and is involved in insect cuticle development},
author = {Y. Duan and W. Zhu and X. Zhao and H. Merzendorfer and J. Chen and X. Zou and Q. Yang},
doi = {10.1016/j.ibmb.2021.103718},
issn = {0965-1748},
year = {2022},
date = {2022-01-01},
journal = {Insect Biochem Mol Biol},
volume = {141},
pages = {103718},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Kottaipalayam-Somasundaram, S. R.; Jacob, J. P.; Aiyar, B.; Merzendorfer, H.; Nambiar-Veetil, M.
Chitin metabolism as a potential target for RNAi-based control of the forestry pest Hyblaea puera Cramer (Lepidoptera: Hyblaeidae) Journal Article
In: Pest Manag Sci, vol. 78, no. 1, pp. 296-303, 2022, ISSN: 1526-498x.
@article{RN14057,
title = {Chitin metabolism as a potential target for RNAi-based control of the forestry pest Hyblaea puera Cramer (Lepidoptera: Hyblaeidae)},
author = {S. R. Kottaipalayam-Somasundaram and J. P. Jacob and B. Aiyar and H. Merzendorfer and M. Nambiar-Veetil},
doi = {10.1002/ps.6634},
issn = {1526-498x},
year = {2022},
date = {2022-01-01},
journal = {Pest Manag Sci},
volume = {78},
number = {1},
pages = {296-303},
keywords = {},
pubstate = {published},
tppubtype = {article}
}