Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Technická 3, Prague 6, 166 28, Czech Republic.
Molecules. 2017 Jun 23;22(7):1038. doi: 10.3390/molecules22071038.
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.
许多碳水化合物结合蛋白在其结合部位含有芳香族氨基酸残基。这些残基通过 CH/π 相互作用以堆积的方式与碳水化合物相互作用。这些相互作用存在于碳水化合物结合蛋白中，包括凝集素、酶和碳水化合物转运蛋白。除此之外，许多非蛋白质芳香族分子（天然的和人工的）也可以通过这些相互作用与糖结合。最近的计算和实验研究表明，碳水化合物-芳香族 CH/π 相互作用是色散相互作用，受静电调节，并在溶剂化体系中部分由疏水效应稳定。
