6533b86cfe1ef96bd12c893b

RESEARCH PRODUCT

Local control of antibody binding to hapten-presenting interfaces: Steric and electrostatic interaction

Mathias LöscheM. PiepenstockHelmuth Möhwald

subject

Steric effectsPolymers and PlasticsChemistryStereochemistryOrganic ChemistryCondensed Matter PhysicsElectrostaticsEpitopePhase (matter)MonolayerMaterials ChemistryBiophysicsFluorescence microscopeMoleculelipids (amino acids peptides and proteins)Hapten

description

The binding of labeled antibodies to hapten substituted monolayers at the air/water interface has been studied by means of fluorescence microscopy. Haptens with various spacer lengths between the epitope and a hydrocarbon chain, anchoring the molecule to the interface, have been synthesized. With DMPC,a unspecific binding has been shown to predominate over specific binding due to electrostatic interactions. At high surface pressures the bound antibody is detached because of steric interference with the lipid head groups. Due to a reduction of electrostatic interactions, no unspecific binding is observed to monolayers of cholesterol, which carries a small dipole moment. Mixed monolayers of cholesterol and DMPC separate into two fluid phases, with preferential antibody binding to the cholesterol-enriched phase.

https://doi.org/10.1002/masy.19910460142