Trifluoroethanol induces the self‐association of specific amphipathic peptides

FEBS Letters

H. Sawyer, William¹  Howlett, Geoffrey J¹  MacPhee, Cait E¹  Perugini, Matthew A¹ 

[1] Russell Grimwade School of Biochemistry and Molecular Biology, University of Melbourne, Parkville, Vic. 3052, Australia

关键词: Apolipoprotein;    α-Helical peptide;    Lipid-peptide interaction;    Trifluoroethanol;    Circular dichroism;    Analytical ultracentrifugation;    TFE;    2;    2;    2-trifluoroethanol;    SDS;    sodium dodecyl sulphate;    apo C-II;    apolipoprotein C-II;    apo E;    apolipoprotein E;    TFA;    trifluoroacetic acid;    MRE;    mean residue ellipticity;    CD;    circular dichroism;   

DOI  :  10.1016/S0014-5793(97)01224-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 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.

【 授权许可】

Unknown