The binding of aromatic derivatives of β-d-galactopyranosides to the fab' of immunoglobulin J539. Observation on the nature of ligand-antibody interactions |
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Authors: | Manoj K. Das Emmanuel Zissis Cornelis P.J. Glaudemans |
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Affiliation: | National Institute of Arthritis, Metabolism, and Digestive Diseases, National Institutes of Health, Bethesda, MD 20205 U.S.A. |
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Abstract: | 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. |
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