CH/π Interactions in Carbohydrate Recognition

作者：Vojtěch Spiwok · 发表于：Molecules · 年份：2017 · DOI：10.3390/molecules22071038 · 被引用次数：141 · 研究领域：Protein Structure and Dynamics、Glycosylation and Glycoproteins Research、Molecular spectroscopy and chirality

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.