TCB Publications - Abstract

Daniel T. Infield, Ali Rasouli, Grace G. Galles, Christophe Chipot, Emad Tajkhorshid, and Christopher A. Ahern. Cation-π interactions and their functional roles in membrane proteins. Journal of Molecular Biology, 433:167035, 2021. (PMC: PMC8338773)

INFI2021-ET Membrane proteins rely on diverse molecular forces to execute essential physiological tasks. Cation- interactions arise as a result of strong attractive forces between positively charged entities and the -electron cloud of aromatic groups. The physicochemical characteristics of cation- interactions are particularly well-suited to the dual hydrophobic/hydrophilic environment of membrane proteins, and they have been shown to play important roles in membrane protein function. As high-resolution structural data of membrane proteins bring molecular features into increasingly sharper view, cation- interactions are gaining traction as essential contributors to membrane protein chemistry, function, and pharmacology. Herein, after briefly reviewing the physicochemical properties of cation- interactions, we present several examples of prominent cation- interactions in ion channels and other membrane proteins, and we highlight their specific functional roles.

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