• amphiphilic peptides;
  • bilayer formation;
  • CD study;
  • conformational properties;
  • liquid-phase peptide synthesis;
  • ß-structure potential

The conformational behaviour of the monodisperse amphiphilic oligopeptides (L-Thr-L-Val)n (I and II) and (L-Ser-L-Leu)n (III) for n = 1–4 was investigated by CD spectroscopy in TFE, MeOH and water. A conformational transition random-coil -> ß-structure was observed for both series: the critical chain length for ß-structure formation turned out to be dependent on solvent and spatial similarity of the amino acid side-chains. The very short critical chain-length for the onset of ß-structure formation for peptides I and II (n = 3) is explained by the formation of bilayer sheets, in which the minimization of hydrophobic contacts between the amphipilic peptide and the hydrophilic solvent represents an important driving force for ß-structure formation. The use of amphiphilic peptides for the construction of artificial proteins is briefly discussed.