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Surface active properties of amphiphilic sequential isopeptides: Comparison between α‐helical and β‐sheet conformations
Author(s) -
MagetDana Régine,
Lelièvre Dominique,
Brack André
Publication year - 1999
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(19990415)49:5<415::aid-bip7>3.0.co;2-j
Subject(s) - chemistry , monolayer , amphiphile , peptide , beta sheet , adsorption , stereochemistry , crystallography , beta (programming language) , organic chemistry , copolymer , biochemistry , computer science , programming language , polymer
Poly(Leu–Lys–Lys–Leu) and poly(Leu–Lys) are sequential amphiphilic peptide isomers that adopt respectively an α‐helical conformation and a β‐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 α‐helical and β‐sheet conformations. Both have a natural tendency to spread at the surface of a saline solution and the values of the equilibrium spreading pressure π e lie in the same range. When dissolved in a saline solution, α‐helical peptides diffuse faster and adsorb faster at the interface than the β‐sheet isomers. From the compression isotherms of LKKL and LK peptide monolayers it is possible to extract parameters that characterize the behavior of α‐helical and β‐sheet conformations: β‐sheet peptide monolayers are more stable and less compressible than the monolayers formed with the α‐helical isomers. The LK peptides differ also by their high degree of self‐association at the air/water interface. © 1999 John Wiley & Sons, Inc. Biopoly 49: 415–423, 1999