Comparative Study of Molecular Interaction of Quercetin and B4S With Kinensin-5 Protein In-Silico for the selective anticancer activity of Quercetin

Abstract

Aim: To study the comparative molecular interactions of Quercetin and 3’-fluoro-4’-(trifluoromethyl)biphenyl-4-sulfonamide (B4S) with the active sites of Kinesin-5 protein using molecular docking analysis for the selective anticancer activity. Materials and Methods: The protein structures are collected from the protein data bank (PDB) website and the ligand structures were collected from the PUBCHEM website.The samples were regarded as (N=10) for Kinensin-5 protein with quercetin and (N=10) for Kinensin-5 protein with B4S according to the sample size calculations performed from clinicalc.com with pretest G power 80%. The total sample size was 20. The binding energy (kcal/mol) was calculated using Autodock vina software. The non-covalent protein ligand interactions were detected using protein–ligand interaction profiler (PLIP) webserver. Results: The mean binding affinity of Quercetin (-9.5 kcal/mol) was significantly (p=<0.001, p<0.05, 2-tailed t-test) higher than B4S (-7.21 kcal/mol) towards the active site aminoacid resiues of Kinensin-5 protein. Conclusion: The results indicate that Quercetine has better binding affinity compared the standard Kinensin-5 inhibitor B4S. Hence it may more selectively bind to the cancerous cells to inhibit their proliferation and can acts as a novel anti-cancer agent.