Interaction of Schiff base with bovine serum albumin: site-specific photocleavage |
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Authors: | Shrivastava H Y Kanthimathi M Nair B U |
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Affiliation: | Chemical Laboratory, Central Leather Research Institute, Adyar, Chennai, 600 020, India. |
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Abstract: | A Schiff-base ligand with donor/acceptor substituents viz. 2, 3-bis?[(2-hydroxy-4-diethylamino) (phenyl) (methylene)]amino?-2-butenedinitrile was synthesized, its binding properties with bovine serum albumin (BSA) and its site-specific photocleavage in the presence of cobaltous chloride have been evaluated. The Schiff-base ligand showed increase in absorption with a 5-nm red shift in the absorption maximum consistent with the binding of Schiff-base ligand to hydrophobic sites on the protein. The binding plot obtained from the absorption titration gives a binding constant of 6.4 +/- 0.3 x 10(4) M(-1). The CD spectrum of BSA in presence of the ligand shows that binding of the ligand leads to a change in the helicity of the protein. This ligand has been found to induce site-specific photocleavage of the protein in the presence of cobaltous chloride. The gel electrophoresis pattern of a photolyzed sample of BSA/Schiff-base ligand/cobaltous chloride shows that protein is cleaved into two polypeptide fragments, indicating site-specific binding for the ligand to the protein. |
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