Department of Chemistry, Iowa State University, Ames, Iowa 50011, United States.
J Org Chem. 2021 Dec 17;86(24):18287-18291. doi: 10.1021/acs.joc.1c02373. Epub 2021 Dec 1.
Thioamide substitution of backbone peptide bonds can probe interactions along the main chain of proteins. Despite theoretical predictions of the enhanced hydrogen bonding propensities of thioamides, previous studies often do not consider the geometric constraints imposed by folded peptide secondary structure. This work addresses drawbacks in previous studies that ignored the geometry dependence and local dielectric properties of thioamide hydrogen bonding and identifies cases where thioamides may be either stronger or weaker hydrogen-bonding partners than amides.
硫酰胺取代骨架肽键可以探测蛋白质主链上的相互作用。尽管理论上预测硫酰胺具有增强的氢键倾向，但以前的研究通常不考虑折叠肽二级结构所施加的几何约束。这项工作解决了以前研究中的缺陷，这些研究忽略了硫酰胺氢键的几何依赖性和局部介电性质，并确定了硫酰胺可能是比酰胺更强或更弱的氢键供体或受体的情况。
