Ordering transitions triggered by specific binding of vesicles to protein-decorated interfaces of thermotropic liquid crystals.

ABSTRACT: We report that specific binding of ligand-functionalized (biotinylated) phospholipid vesicles (diameter = 120 ± 19 nm) to a monolayer of proteins (streptavidin or anti-biotin antibody) adsorbed at an interface between an aqueous phase and an immiscible film of a thermotropic liquid crystal (LC) [nematic 4'-pentyl-4-cyanobiphenyl (5CB)] triggers a continuous orientational ordering transition (continuous change in the tilt) in the LC. Results presented in this paper indicate that, following the capture of the vesicles at the LC interface via the specific binding interaction, phospholipids are transferred from the vesicles onto the LC interface to form a monolayer, reorganizing and partially displacing proteins from the LC interface. The dynamics of this process are accelerated substantially

SUBMITTER: Tan LN 

PROVIDER: S-EPMC3359374 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature