CH–π interaction between cross-strand amino acid pairs stabilizes β-hairpins. Issue 92 (4th November 2020)

• Record Type: Journal Article
• Authors: Ghosh, Pritha; Chatterjee, Jayanta
• Is Part Of: Chemical communications. Volume 56:Issue 92(2020)
• Page Start: 14447
• Page End: 14450
• Publication Date: 2020-11-04
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/d0cc05653g
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : We identified several CH–π donor–acceptor pairs involving amino acid side chains with less polarized C–H bonds at a solvent-exposed site between the strands of a β-hairpin peptide. Abstract : We identified several CH–π donor–acceptor pairs involving amino acid side chains with less polarized C–H bonds at a solvent-exposed site between the strands of a β-hairpin peptide. Therein, we observe a distance-dependent induction of CH–π interaction within the aliphatic-aromatic amino acid pair. Our results also suggest an interplay of hydrophobicity and CH–π interaction in dictating the stability of β-hairpins, where a leucine-tryptophan pair contributes −1.14 kcal mol −1 to the overall foldedness of the β-hairpin.