Spectroscopic, molecular docking and dynamic simulation studies of binding between the new anticancer agent olmutinib and human serum albumin

Abstract

In this study, the interaction between human serum albumin (HSA), which is the key bio-distributor of exogenous and endogenous compounds in the human bloodstream, and HM61713 (Olmutinib; OMB), which is used as an anticancer drug, is examined by multiple spectroscopic techniques (steady-state fluorescence, UV spectrophotometry, synchronous, and 3 D fluorescence) combined with molecular docking and molecular dynamic simulation investigations. The fluorescence results clearly demonstrated quenching in HSA fluorescence in the existence of OMB indicating the formation of complex and have also shown that the interaction is static. Fluorescence spectroscopy was used to obtain the binding constant values that revealed a strong interaction between the HSA and OMB at 298 K with a binding constant of 7.39x10⁴ M⁻¹ suggesting strong interaction. OMB binds to HSA at site I (IIA). Electrostatic forces and H-bonding were the main binding forces of main bonding between HSA and OMB as revealed by docking and thermodynamic results.

Communicated by Ramaswamy H. Sarma

Keywords:

• Olmutinib
• Human serum albumin
• Molecular dynamic simulation
• Molecular docking

Acknowledgements

The authors would like to extend their sincere appreciation to the Researchers Support Project number (RSP-2021/261), King Saud University, Riyadh, Saudi Arabia

Disclosure statement

No potential conflict of interest was reported by the author(s).

Additional information

Funding

This work was financially supported by the Researchers Support Project number (RSP-2021/261), King Saud University, Riyadh, Saudi Arabia.