For Part II of this series see (18).
Sequence-dependence of secondary structure formation
III. ß-Structure forming potential of amphiphilic oligopeptides containing alternating L-Val-L-Thr and L-Leu-L-Ser residues*
Article first published online: 12 JAN 2009
© 1986 Munksgaard International Publishers Ltd.
International Journal of Peptide and Protein Research
Volume 27, Issue 3, pages 314–319, March 1986
How to Cite
ALTMANN, K.-H., FLÖORSHEIMER, A. and MUTTER, M. (1986), Sequence-dependence of secondary structure formation. International Journal of Peptide and Protein Research, 27: 314–319. doi: 10.1111/j.1399-3011.1986.tb01826.x
- Issue published online: 12 JAN 2009
- Article first published online: 12 JAN 2009
- Recieved 3 June accepted 30 August 1985
- 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.