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Maget-Dana, R; Lelièvre, D; Brack, A

Surface active properties of amphiphilic sequential isopeptides: Comparison between a-helical and ß-sheet conformations

Biopolymers 49 (5) 415-423

by Administrateur - published on


Poly(Leu-Lys-Lys-Leu) and poly(Leu-Lys) are sequential amphiphilic peptide isomers that adopt respectively an a-helical conformation and a ß-sheet structure in saline solutions and at rite 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 a-helical and ß-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, a-helical peptides diffuse faster and adsorb faster at the interface than the ß-sheet isomers.