化学
残留物(化学)
肽
卤键
分子内力
分子力学
计算化学
拟肽
组合化学
分子动力学
卤素
生物化学
立体化学
有机化学
烷基
作者
Jintian Li,Liping Zhou,Zhong‐Jie Han,Leyun Wu,Jianfang Zhang,Weiliang Zhu,Zhijian Xu
标识
DOI:10.1021/acs.jmedchem.3c02359
摘要
Halogen bonds (XBs) are essential noncovalent interactions in molecular recognition and drug design. Current studies on XBs in drug design mainly focus on the interactions between halogenated ligands and target proteins, lacking a systematic study of naturally existing and artificially prepared halogenated residue XBs (hr_XBs) and their characteristics. Here, we conducted a computational study on the potential hr_XBs in proteins/peptides using database searching, quantum mechanics calculations, and molecular dynamics simulations. XBs at the protein-peptide interaction interfaces are found to enhance their binding affinity. Additionally, the formation of intramolecular XBs (intra_XBs) within proteins may significantly contribute to the structural stability of structurally flexible proteins while having a minor impact on proteins with inherently high structural rigidity. Impressively, introducing halogens without the formation of intra_XBs may lead to a decrease in the protein structural stability. This study enriches our understanding of the roles and effects of halogenated residue XBs in biological systems.
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