Investigates interaction between abscisic acid and bovine serum albumin using various spectroscopic and in-silico techniques

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 H-1 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. (C) 2020 Elsevier B.V. All rights reserved.

Automated summary

The study investigated the binding interaction and mechanism of abscisic acid with bovine serum albumin in physiological solution, showing a static and spontaneous binding nature. Various spectroscopic methods and computational techniques were used to confirm the interaction, supported by fluorescence, UV-Visible absorption, H-1 NMR, molecular docking, and molecular dynamics studies. These findings could be beneficial for the transportation and distribution of abscisic acid in the human body.