Bovine Serum Albumin Interaction with Glycyrrhizin Studiedby UV-Vis Spectroscopy and Molecular Docking

In this research, the interaction of glycyrrhizin (GL) with bovine serum albumin (BSA) has beeninvestigated by UV–Visible spectroscopy and molecular docking simulation. The UV–visible spectroscopicmethod and molecular modeling were performed to determine the binding constant and the binding structureof the GL-BSA complex, respectively. The results of UV–visible spectroscopy showed that GL bonded to BSAwith a binding constant of KGL-BSA = 49.4 (9090.) × 104Lmol-1. The results of molecular docking revealeda minimized affinity value for the first pose of GL-BSA, which was -1192.kcalmol-1, and four amino acids(Tyr156, Thr183, Lys184, and Ala2.0) exhibited high affinity with GL. The GL-BSA complex primarilyforms based on hydrogen bonds.

Bovine Serum Albumin Interaction with Glycyrrhizin Studiedby UV-Vis Spectroscopy and Molecular Docking Keywords:

Binding constant , Docking , UV , Visible , Bovine serum albumin , Glycyrrhizin