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Homo‐ and Heterovalent Neoglycoproteins as Ligands for Bacterial Lectins

Homo‐ and Heterovalent Neoglycoproteins as Ligands for Bacterial Lectins Click chemistry gives access to unlimited set of multivalent glycoconjugates to explore carbohydrate‐protein interactions and discover high affinity ligands. In this study, we have created supramolecular systems based on a carrier protein that was grafted by Cu(I)‐catalyzed azide‐alkyne cycloaddition with tetravalent glycodendrons presenting αGal, βGal and/or αFuc. Binding studies of the homo‐ (4 a–c) and heterovalent (5) neoglycoproteins (neoGPs) with the LecA and LecB lectins from P. aeruginosa has first confirmed the interest of the multivalent presentation of glycodendrons by the carrier protein (IC50 up to 2.8 nM). Moreover, these studies have shown that the heterovalent display of glycans (5) allows the interaction with both lectins (IC50 of 10 nM) despite the presence of unspecific moieties, and even with similar efficiency for LecB. These results demonstrate the potential of multivalent and multispecific neoGPs as a promising strategy to fight against resistant pathogens. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png ChemPlusChem Wiley

Homo‐ and Heterovalent Neoglycoproteins as Ligands for Bacterial Lectins

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Publisher
Wiley
Copyright
© 2022 Wiley‐VCH GmbH
eISSN
2192-6506
DOI
10.1002/cplu.202100481
Publisher site
See Article on Publisher Site

Abstract

Click chemistry gives access to unlimited set of multivalent glycoconjugates to explore carbohydrate‐protein interactions and discover high affinity ligands. In this study, we have created supramolecular systems based on a carrier protein that was grafted by Cu(I)‐catalyzed azide‐alkyne cycloaddition with tetravalent glycodendrons presenting αGal, βGal and/or αFuc. Binding studies of the homo‐ (4 a–c) and heterovalent (5) neoglycoproteins (neoGPs) with the LecA and LecB lectins from P. aeruginosa has first confirmed the interest of the multivalent presentation of glycodendrons by the carrier protein (IC50 up to 2.8 nM). Moreover, these studies have shown that the heterovalent display of glycans (5) allows the interaction with both lectins (IC50 of 10 nM) despite the presence of unspecific moieties, and even with similar efficiency for LecB. These results demonstrate the potential of multivalent and multispecific neoGPs as a promising strategy to fight against resistant pathogens.

Journal

ChemPlusChemWiley

Published: Feb 1, 2022

Keywords: bacterial lectin; click chemistry; glycodendrimer; multivalency; neoglycoprotein

References