Trifluoroethanol induces the self-association of specific amphipathic peptides

C E MacPhee, M A Perugini, W H Sawyer, G J Howlett, Cait MacPhee

Research output: Contribution to journalArticlepeer-review

Abstract

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-NH2), remained monomeric under conditions where TFE induced a two-state transition from a random coil to an alpha-helix, In contrast, the TEE-induced alpha-helical formation of two peptides derived from human apolipoproteins CII 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. (C) 1997 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)265-268
Number of pages4
JournalFEBS Letters
Volume416
Issue number3
DOIs
Publication statusPublished - 27 Oct 1997

Keywords

  • apolipoprotein
  • alpha-helical peptide
  • lipid-peptide interaction
  • trifluoroethanol
  • circular dichroism
  • analytical ultracentrifugation
  • GCN4 LEUCINE-ZIPPER
  • SECONDARY STRUCTURE
  • QUATERNARY STRUCTURE
  • AQUEOUS-SOLUTION
  • COILED COILS
  • PROTEIN
  • HELIX
  • SEQUENCE
  • MUTANTS

Fingerprint

Dive into the research topics of 'Trifluoroethanol induces the self-association of specific amphipathic peptides'. Together they form a unique fingerprint.

Cite this