CD spectroscopy analyses of peptides. CD spectroscopic results of gHH1, gHH2, gHH3, gHH5 and gBH1 in PBS solution with 0%, 20%, 40%, 80% TEF, respectively. The gHH1, gHH3 and gBH1 peptides adopted a standard α-helical conformation with double minima at 208 nm and 222 nm in a PBS-buffered solution and remained practically unaltered in the presence of TFE. CD analysis of gHH2 showed that the peptide adopted a β-sheet conformation in buffer solution, and its CD spectra remained practically unaltered in TFE solution. gHH5 had a structural change from random coil to α-helical structure when the peptide was transferred from a polar environment to membrane interfaces using aqueous mixtures of TFE.