BINDING OF AROMATIC DERIVATIVES OF BETA-D-GALACTOPYRANO-SIDES TO THE FAB' OF IMMUNOGLOBULIN-J539 - OBSERVATIONS ON THE NATURE OF LIGAND-ANTIBODY INTERACTIONS

A number of d-galactopyranosides bearing aromatic substituents have been prepared, and their binding to immunoglobulin J539 (Fab') has been studied. It appears that the main contribution of the 6-O-aromatic moiety to binding arises from the fact that it imparts an increased hydrophobicity to the ligand, causing a decrease in its hydration (solubility) that results in a greater free-energy of binding. In the d-galactosides having an aromatic aglycon, the phenyl group appears to partake in actual interactions with the protein. © 1979.