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Surface active properties of amphiphilic sequential isopeptides: Comparison between alpha-helical and beta-sheet conformations.
- Source :
-
Biopolymers [Biopolymers] 1999 Apr 15; Vol. 49 (5), pp. 415-423. - Publication Year :
- 1999
-
Abstract
- Poly(Leu-Lys-Lys-Leu) and poly(Leu-Lys) are sequential amphiphilic peptide isomers that adopt respectively an alpha-helical conformation and a beta-sheet structure in saline solutions and at the air/water interface. The surface active properties of LKKL and LK sequential isopeptides containing 16, 20, and n residues have been compared in order to evaluate the contributions of the alpha-helical and beta-sheet conformations. Both have a natural tendency to spread at the surface of a saline solution and the values of the equilibrium spreading pressure pi(e) lie in the same range. When dissolved in a saline solution, alpha-helical peptides diffuse faster and adsorb faster at the interface than the beta-sheet isomers. From the compression isotherms of LKKL and LK peptide monolayers it is possible to extract parameters that characterize the behavior of alpha-helical and beta-sheet conformations: beta-sheet peptide monolayers are more stable and less compressible than the monolayers formed with the alpha-helical isomers. The LK peptides differ also by their high degree of self-association at the air/water interface. Copyright 1999 John Wiley & Sons, Inc.
Details
- Language :
- English
- ISSN :
- 1097-0282
- Volume :
- 49
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Biopolymers
- Publication Type :
- Academic Journal
- Accession number :
- 11180048
- Full Text :
- https://doi.org/10.1002/(SICI)1097-0282(19990415)49:5<415::AID-BIP7>3.0.CO;2-J