Premium
Local control of antibody binding to hapten‐presenting interfaces: Steric and electrostatic interaction
Author(s) -
Piepenstock Michael,
Lösche Mathias,
Möhwald Helmuth
Publication year - 1991
Publication title -
makromolekulare chemie. macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 0258-0322
DOI - 10.1002/masy.19910460142
Subject(s) - hapten , monolayer , steric effects , chemistry , binding site , dipole , fluorescence , crystallography , stereochemistry , biophysics , antibody , biochemistry , organic chemistry , biology , physics , quantum mechanics , immunology
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.