Comparative Study of Molecular Interactions of Thymol and B4S with Kinesin-5 In-Silico for the Selective Anti-cancer Activity of Thymol

Abstract

Aim: To study the comparative molecular interactions of Thymol and 3’-fluoro-4’-(trifluoromethyl)biphenyl-4-sulfonamide (B4S) with the active sites of Kinesin-5 protein using molecular docking analysis for the selective anti-cancer activity. Materials and Methods: In this study, Group 1 is the binding affinity of B4S with Kinesin-5 protein and Group 2 is the binding affinity of Thymol with Kinesin-5 protein. The sample size was calculated with a pretest power of 80%. The sample size per group is 10 and the total sample size is 20. The protein structure of Kinesin-5 protein was collected from the protein data bank (PDB) website and the ligand structures were collected from the NCBI-PubChem website. The binding energy (kcal/mol) was calculated using Autodock Vina Software.The structure of the protein was obtained from the PDB (protein data bank) database and the structures of ligand were obtained from the NCBI-PubChem database. The binding energy (kcal/mol) was calculated using Novel Autodock Vina Software. Results: The mean binding affinity of Thymol (-7.89 kcal/mol) was significantly (p=0.007, p<0.05, 2-tailed t-test) higher than the standard inhibitor B4S (-7.19 kcal/mol) towards the active sites of Kinesin-5 protein. Conclusion: The results suggest that thymol may bind selectively to the cancerous cells and inhibit their proliferation and can act as a novel anti-cancer agent.