INVESTIGATION ON THE INTERACTION OF β-SITOSTEROL AND LUTEOLIN-7-GLUCOSIDE BINDING TO BOVINE SERUM ALBUMIN

Objective: The study ondrug–protein interactions is an important field of interest because the prospective unraveling drug action mechanisms and possibility designing novel medicines. Bovine serum albumin (BSA) has been studied extensively its structural homology with human (HSA). objective work was to interaction between β-sitosterol Luteolin–7-glucoside bovine investigated by molecular docking. Methods: Docking studies were carried out using a crystal structure complexed naproxen (pdb code-4OR0). Auto dock 4.2 used perform Ligands found flexible during docking process, protein kept rigid. Results: Molecular revealed that can bind in large hydrophobic cavity BSA, mainly but also hydrogen bond hydroxyl (OH) group SER 488 distance 2.1Å. Luteolin-7-glucoside molecule interact LYS 431, ARG 427, ALA 193 amino acids Serum Albumin. 458, 435, 185 are involved forming oxygens, carbonyl carbon 2.4, 2.3 1.9 Å, respectively. Conclusion: Study indicated bonding mostly responsible for interaction. Further research pharmaceutical potential plant molecules will be valuable monitoring their biological functions.