Peptide adsorption to lipid bilayers: slow processes revealed by linear dichroism spectroscopy.

ABSTRACT: The adsorption and insertion kinetics for the association of two 34-residue cyclic peptides with phosphocholine membranes have been studied using circular and linear dichroism approaches. The two peptides studied are identical with the exception of two residues, which are both tyrosine in one of the peptides and tryptophan in the other. Both peptides adopt random coil conformations in solution in the absence of membranes and do not aggregate at concentrations below 20 microM. After addition to liposome dispersions, circular dichroism spectroscopy indicated that both peptides undergo an extremely rapid transformation to a beta-conformation that remains unchanged throughout the remainder of the experiment. Linear dichroism (LD) spectroscopy was used to study the kinetics of membrane adsorpti

SUBMITTER: Ennaceur SM 

PROVIDER: S-EPMC2717241 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature