Abstract
Cation-π interactions arise as a result of strong attractive forces between positively charged entities and the π-electron cloud of aromatic groups. The physicochemical characteristics of cation-π 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-π interactions are gaining traction as essential contributors to membrane protein chemistry, function, and pharmacology. Here we review the physicochemical properties of cation-π interactions and present several prominent examples which demonstrate significant roles for this specialized biological chemistry.
| Original language | English (US) |
|---|---|
| Article number | 167035 |
| Journal | Journal of Molecular Biology |
| Volume | 433 |
| Issue number | 17 |
| DOIs | |
| State | Published - Aug 20 2021 |
Keywords
- GPCR
- cation-π interactions
- computational chemistry
- genetic code expansion
- ion channels
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Molecular Biology
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