| Autor: |
Mark L. McLaughlin, Robert P. Hammer, Lars G. J. Hammarström, Ted J. Gauthier |
| Rok vydání: |
2001 |
| Předmět: |
|
| Zdroj: |
The Journal of Peptide Research. 58:108-116 |
| ISSN: |
1397-002X |
| DOI: |
10.1034/j.1399-3011.2001.00858.x |
| Popis: |
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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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