The conformation of de novo designed amphiphilic peptides with six or nine L-2-(2,2,2-trifluoroethyl)glycines as the hydrophobic amino acid

Article abstract of DOI:10.1246/bcsj.73.439

Amphiphilic 21-peptides with six and nine L-2-(2,2,2- trifluoroethyl)glycines as the hydrophobic amino acids and lysine and glutamic acid as the hydrophilic amino acids were synthesized. The CD spectra showed that these peptides with L-2-(2,2,2-trifluoroethyl)glycines took a random conformation in H₂O. On the contrary, similar amphiphilic 21-peptides with leucine as the hydrophobic amino acids took a helical conformation in H₂O. The peptides with L-2-(2,2,2-trifluoroethyl)glycines took a helical conformation in H₂O containing a > 20% volume of 2,2,2-trifluoroethanol. These facts suggested the hydrophobic nature of the L-trifluoroethylglycines. The peptide with six L-2-(2,2,2-trifluoroethyl)glycines took a helical structure in methanol, however it slowly changed into the β-structure within 24 h. Interestingly, the peptide with nine L-2-(2,2,2-trifluoroethyl)glycines formed a stable helix under the same conditions. The peptide with nine L-2- (2,2,2-trifluoroethyl)glycines preferred a helical structure, probably because the assembling of the Tfeg side chains was more effective in forming its helix rather than the β-structure.