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Trifluoroethanol induces the self‐association of specific amphipathic peptides
Author(s) -
MacPhee Cait E,
Perugini Matthew A,
H. Sawyer William,
Howlett Geoffrey J
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01224-6
Subject(s) - chemistry , random coil , amphiphile , peptide , monomer , intramolecular force , hydrogen bond , heptad repeat , stereochemistry , circular dichroism , biophysics , peptide sequence , crystallography , biochemistry , molecule , organic chemistry , polymer , biology , copolymer , gene
We have examined the effect of trifluoroethanol (TFE) on the solution behaviour of three amphipathic peptides. One of the peptides, containing three heptad repeat units (Ac‐YS‐(AKEAAKE) 3 GAR‐NH 2 ), remained monomeric under conditions where TFE induced a two‐state transition from a random coil to an α‐helix. In contrast, the TFE‐induced α‐helical formation of two peptides derived from human apolipoproteins C‐II and E was accompanied by the formation of discrete dimers and trimers, respectively. The apolipoprotein C‐II peptide further aggregated to form β‐sheet at higher concentrations of TFE (50% v/v). The results suggest a class of peptides capable of discrete self‐association in the presence of cosolvents which favour intramolecular hydrogen bonding.