The binding of aromatic derivatives of beta-D-galactopyranosides 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.
D005697:Galactosides; D006027:Glycosides; D007140:Immunoglobulin Fab Fragments; D007700:Kinetics; D008024:Ligands; D008958:Models, Molecular; D008968:Molecular Conformation; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship
D005697:Galactosides; D006027:Glycosides; D007140:Immunoglobulin Fab Fragments; D008024:Ligands