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Several biological processes in the body involve the ligand-protein association and thereby exert a wide spectrum of pharmaceutical activities. Consequently, the research community worked hard for a long time to explore the phenomenon of drug-protein binding. Insights into the molecular and physiological processes of a flavonoid, galangin (GAL) upon binding to human serum albumin (HSA) have been explored  in vitro  via both experimental and theoretical approaches. GAL is a natural, multifunctional and a potential anticancer drug and HSA is a plentiful protein in the circulatory system of humans. UV absorption, calorimetric, temperature-dependent ellipticity, fluorescence lifetime decay, FRET, electrochemical, zeta potential and in silico studies were used to further investigate GAL-HSA interaction. Results of these investigations suggested the interaction between GAL and HSA. The location of GAL on HSA was identified by site probe experiments and further confirmed by molecular docking and simulation studies.

analytical chemistry letters

Biophysical, Calorimetric, Zeta Potential, Voltammetric and Computational Insights into the Interaction of An Antimuta-genic Agent with Human Serum Albumin