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CH−π Interactions in Glycan Recognition

Cite this: ACS Chem. Biol. 2021, 16, 10, 1884–1893
Publication Date (Web):October 6, 2021
https://doi.org/10.1021/acschembio.1c00413
Copyright © 2021 American Chemical Society

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    Abstract

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    Carbohydrate recognition is crucial for biological processes ranging from development to immune system function to host–pathogen interactions. The proteins that bind glycans are faced with a daunting task: to coax these hydrophilic species out of water and into a binding site. Here, we examine the forces underlying glycan recognition by proteins. Our previous bioinformatic study of glycan-binding sites indicated that the most overrepresented side chains are electron-rich aromatic residues, including tyrosine and tryptophan. These findings point to the importance of CH−π interactions for glycan binding. Studies of CH−π interactions show a strong dependence on the presence of an electron-rich π system, and the data indicate binding is enhanced by complementary electronic interactions between the electron-rich aromatic ring and the partial positive charge of the carbohydrate C–H protons. This electronic dependence means that carbohydrate residues with multiple aligned highly polarized C–H bonds, such as β-galactose, form strong CH−π interactions, whereas less polarized residues such as α-mannose do not. This information can guide the design of proteins to recognize sugars and the generation of ligands for proteins, small molecules, or catalysts that bind sugars.

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    This article is cited by 18 publications.

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