The binding and diffusion of two model membrane-active peptides at a phospholipid bilayer interface were measured using single-molecule burst-counting methods and autocorrelation analysis. Hydrophobic considerations predict that both peptides should possess similar adsorption free energies. Significant differences in the adsorption and diffusion of the two model peptides are observed and are attributed to peptide-specific interactions with the bilayer. These studies illustrate the power and promise of single molecule methods to reveal details about binding and transport of peptides at cellular interfaces.
Web Page: www.chem.umd.edu/groups/english/
Back to Spectroscopy of Biomolecules, Inferfaces and Materials II
Back to The 37th Middle Atlantic Regional Meeting (May 22-25, 2005)