Key Laboratory of Pesticide & Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University, Wuhan 430079, PR China; International Joint Research Center for Intelligent Biosensor Technology and Health, Central China Normal University, Wuhan 430079, PR China; State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, PR China.
Key Laboratory of Pesticide & Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University, Wuhan 430079, PR China; International Joint Research Center for Intelligent Biosensor Technology and Health, Central China Normal University, Wuhan 430079, PR China.
Drug Discov Today. 2023 May;28(5):103546. doi: 10.1016/j.drudis.2023.103546. Epub 2023 Mar 5.
As major forces for modulating protein folding and molecular recognition, cation and π interactions are extensively identified in protein structures. They are even more competitive than hydrogen bonds in molecular recognition, thus, are vital in numerous biological processes. In this review, we introduce the methods for the identification and quantification of cation and π interactions, provide insights into the characteristics of cation and π interactions in the natural state, and reveal their biological function together with our developed database (Cation and π Interaction in Protein Data Bank; CIPDB; http://chemyang.ccnu.edu.cn/ccb/database/CIPDB). This review lays the foundation for the in-depth study of cation and π interactions and will guide the use of molecular design for drug discovery.
作为调节蛋白质折叠和分子识别的主要力量，阳离子和π相互作用在蛋白质结构中被广泛识别。它们在分子识别中比氢键更具竞争力，因此在许多生物过程中至关重要。在这篇综述中，我们介绍了识别和量化阳离子和π相互作用的方法，深入了解了自然状态下阳离子和π相互作用的特点，并结合我们开发的数据库（蛋白质数据银行中的阳离子和π相互作用；CIPDB；http://chemyang.ccnu.edu.cn/ccb/database/CIPDB）揭示了它们的生物学功能。这篇综述为深入研究阳离子和π相互作用奠定了基础，并将指导药物发现中的分子设计。
