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

Amphiphilic 21-peptides with six and nine L-2-(2,2,2-trifluoroethyl)glycine s as the hydrophobic amino acids and lysine and glutamic acid as the hydrop hilic amino acids were synthesized. The CD spectra showed that these peptid es with L-2-(2,2,2-trifluoroethyl)glycines took a random conformation in H2 O. On the contrary, similar amphiphilic 21-peptides with leucine as the hyd rophobic amino acids took a helical conformation in H2O. The peptides with L-2-(2,2,2-trifluoroethyl)glycines took a helical conformation in H2O conta ining a > 20% volume of 2,2,2-trifluoroethanol. These facts suggested the h ydrophobic nature of the L-trifluoroethylglycines. The peptide with six L-2 -(2,2,2-trifluoroethyl)glycines took a helical structure in methanol, howev er it slowly changed into the beta-structure within 24 h. Interestingly, th e peptide with nine L-2-(2,2,2-trifluoroethyl)glycines formed a stable heli x under the same conditions. The peptide with nine L-2-(2,2,2-trifluoroethy l)glycines preferred a helical structure, probably because the assembling o f the Tfeg side chains was more effective in forming its helix rather than the beta-structure.