Abstract
The binding interaction and binding mechanism of abscisic acid with bovine serum albumin (BSA) in physiological solution (Phosphate buffer pH 7.4) have been studied using various spectroscopic methods in combination with in-silico techniques. The fluorescence data has shown abscisic acid has strongly quenched the intrinsic fluorescence of bovine serum albumin due to the formation of abscisic acid-BSA complex and binding was found to be static and spontaneous in nature. The UV-Visible absorption and 1H NMR studies have also indicated the interaction of abscisic acid with BSA. Finally, the molecular docking and molecular dynamics studies have also shown the stable interaction of abscisic acid with the amino acids of BSA. In conclusion, these findings could be beneficial and supports for the transportation, distribution of abscisic acid in human body.
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