Alcohol-Induced Helix-Sheet Transition of a Sequential Alternating Amphiphilic Polypeptide

The conformation of poly(Glu-Leu-Lys-Leu) was converted a (beta)-sheet to an (alpha)-helix by addition of alcohols. The polypeptide has two HFIP-induced conformational transitional points. The non-hydrogen bonded interactions, the hydrophobicity of the peptide surface, and the secondary structural propensities of the constituent amino acids would play a major role in the conformational transitions and secondary structural stability.