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Demixing of water and ethanol causes conformational redistribution and gelation of the cationic GAG tripeptide.

Research paper by Bridget B Milorey, Stefanie S Farrell, Siobhan E SE Toal, Reinhard R Schweitzer-Stenner

Indexed on: 29 Sep '15Published on: 29 Sep '15Published in: Chemical Communications



Abstract

The cationic tripeptide GAG undergoes three conformational changes in binary mixtures of water and ethanol. At 17 mol% of ethanol conformational sampling is shifted from pPII towards β-strands. A more pronounced shift in the same direction occurs at 40 mol%. At ca. 55 mol% of ethanol and above a peptide concentration of ca. 0.2 M the ternary peptide-water-ethanol mixture forms a hydrogel which is comprised of unusually large crystalline like non-β sheet fibrils forming a sample spanning matrix.