Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 433, Issue 17, Pages -Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2021.167035
Keywords
cation-pi interactions; computational chemistry; ion channels; GPCR; genetic code expansion
Categories
Funding
- Agence National de la Recherche
- NIH [NIH F32HL149184, NIH P41-GM104601, R24-NS104617]
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Cation-pi interactions arise from the strong attraction between positively charged entities and the pi-electron cloud of aromatic groups, making them well-suited to the hydrophobic/hydrophilic environment of membrane proteins. As high-resolution structural data of membrane proteins become clearer, cation-pi interactions are increasingly recognized as essential contributors to membrane protein chemistry, function, and pharmacology. Prominent examples demonstrate the significant roles of cation-pi interactions in specialized biological chemistry.
Cation-pi interactions arise as a result of strong attractive forces between positively charged entities and the pi-electron cloud of aromatic groups. The physicochemical characteristics of cation-pi interactions are particularly well-suited to the dual hydrophobic/hydrophilic environment of membrane proteins. As high-resolution structural data of membrane proteins bring molecular features into increasingly sharper view, cation-pi interactions are gaining traction as essential contributors to membrane protein chemistry, function, and pharmacology. Here we review the physicochemical properties of cation-pi interactions and present several prominent examples which demonstrate significant roles for this specialized biological chemistry. (C) 2021 Published by Elsevier Ltd.
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