Insight into indole interactions from alkali metal chloride effects on a tryptophan zipper beta-hairpin peptide

Journal of the American Chemical Society
Christopher E Dempsey, Philip E Mason

Abstract

Weakly solvated, low charge density, alkali metal cations (K+ and Rb+) destabilize tryptophan zipper (trpzip) peptides with an effectiveness (for Rb+) similar to that of the protein denaturant urea. An analysis of alkali metal cation effects on polypeptides stabilized predominantly either by hydrogen bonds or by the classical hydrophobic effect indicates that the alkali metals attenuate stabilizing interactions involving the tryptophan indole groups. Destabilization does not result from electrolyte screening of the electrostatic component of the indole-indole interaction, but is likely to involve direct interaction of the low charge density cation with the indole group in a cation-pi interaction. The observations highlight a general simplicity in the nature of molecular interactions in solution, in which stabilizing contributions to polypeptide and protein structures are attenuated by solutes of a complementary nature.

References

May 2, 2001·Proceedings of the National Academy of Sciences of the United States of America·A G CochranM A Starovasnik
Apr 10, 2003·Proceedings of the National Academy of Sciences of the United States of America·P E MasonJ M Cruickshank
Jan 12, 2005·Biochemistry·Christopher E DempseyPhilip E Mason

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Citations

Oct 31, 2009·Journal of the American Chemical Society·Philip E MasonJohn W Brady
May 31, 2007·Chemical Communications : Chem Comm·Surajit GhoshSandeep Verma
Apr 12, 2016·Organic & Biomolecular Chemistry·Maruthi KondaApurba K Das
Oct 19, 2007·Chemistry : a European Journal·Clara M SantiveriM Angeles Jiménez
Jun 22, 2010·Biopolymers·Clara M Santiveri, M Angeles Jiménez
Dec 7, 2007·Journal of the American Chemical Society·Christopher E DempseyGeorge W Neilson

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