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Molecules 2017, 22(7), 1038; doi:10.3390/molecules22071038

CH/π Interactions in Carbohydrate Recognition

Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Technická 3, Prague 6, 166 28, Czech Republic
Received: 11 May 2017 / Revised: 11 June 2017 / Accepted: 21 June 2017 / Published: 23 June 2017
(This article belongs to the Special Issue Protein-Carbohydrate Interactions)
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Abstract

Many carbohydrate-binding proteins contain aromatic amino acid residues in their binding sites. These residues interact with carbohydrates in a stacking geometry via CH/π interactions. These interactions can be found in carbohydrate-binding proteins, including lectins, enzymes and carbohydrate transporters. Besides this, many non-protein aromatic molecules (natural as well as artificial) can bind saccharides using these interactions. Recent computational and experimental studies have shown that carbohydrate–aromatic CH/π interactions are dispersion interactions, tuned by electrostatics and partially stabilized by a hydrophobic effect in solvated systems. View Full-Text
Keywords: carbohydrate-protein interactions; CH/π interactions; lectins; interaction energy; non-canonical hydrogen bond carbohydrate-protein interactions; CH/π interactions; lectins; interaction energy; non-canonical hydrogen bond
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Spiwok, V. CH/π Interactions in Carbohydrate Recognition. Molecules 2017, 22, 1038.

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