Trifluoroethanol induces the self-association of specific amphipathic peptides.
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)3GAR-NH2), remained monomeric under conditions where TFE induced a two-state transition from a random coil to an alpha-helix. In contrast, the TFE-induced alpha-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 beta-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.
MacPhee
C E
CE
Russell Grimwade School of Biochemistry and Molecular Biology, University of Melbourne, Parkville, Vic., Australia.
Perugini
M A
MA
Sawyer
W H
WH
Howlett
G J
GJ
D000595:Amino Acid Sequence; D053304:Apolipoprotein C-II; D001056:Apolipoproteins C / Q000737:chemistry* / Q000187:drug effects; D001057:Apolipoproteins E / Q000737:chemistry* / Q000187:drug effects; D002942:Circular Dichroism; D006801:Humans; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000187:drug effects; D010455:Peptides / Q000737:chemistry* / Q000187:drug effects; D017433:Protein Structure, Secondary; D014270:Trifluoroethanol / Q000494:pharmacology*; D014783:Viscosity
D053304:Apolipoprotein C-II; D001056:Apolipoproteins C; D001057:Apolipoproteins E; D010446:Peptide Fragments; D010455:Peptides; D014270:Trifluoroethanol