Amphipathic control of the 3(10)-/alpha-helix equilibrium in synthetic peptides

A series of short, amphipathic peptides incorporating 80% C(alpha),C(alpha)-disubstituted glycines has been prepared to investigate amphipathicity as a helix-stabilizing effect. The peptides were designed to adopt 3(10)- or alpha-helices based on amphipathic design of the primary sequence. Character...

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Bibliographic Details
Published in:The journal of peptide research 2001-08, Vol.58 (2), p.108-116
Main Authors: Hammarström, L G, Gauthier, T J, Hammer, R P, McLaughlin, M L
Format: Article
Language:English
Subjects:
Circular Dichroism
Peptides - chemical synthesis
Peptides - chemistry
Protein Structure, Secondary
Temperature
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Summary:A series of short, amphipathic peptides incorporating 80% C(alpha),C(alpha)-disubstituted glycines has been prepared to investigate amphipathicity as a helix-stabilizing effect. The peptides were designed to adopt 3(10)- or alpha-helices based on amphipathic design of the primary sequence. Characterization by circular dichroism spectroscopy in various media (1 : 1 acetonitrile/water; 9 : 1 acetonitrile/water; 9 : 1 acetonitrile/TFE; 25 mM SDS micelles in water) indicates that the peptides selectively adopt their designed conformation in micellar environments. We speculate that steric effects from ith and ith + 3 residues interactions may destabilize the 3(10)-helix in peptides containing amino acids with large side-chains, as with 1-aminocyclohexane-1-carboxylic acid (Ac(6)c). This problem may be overcome by alternating large and small amino acids in the ith and ith + 3 residues, which are staggered in the 3(10)-helix.
ISSN:1397-002X
DOI:10.1034/j.1399-3011.2001.00858.x