Molecular Docking and Molecular Dynamics Simulation Study of Creatinine Interaction with Human Protein 7XTQ

Creatinine is an endogenous metabolic by-product widely employed as a clinical biomarker for renal function assessment. Despite its physiological importance, limited information is available regarding its molecular-level interaction behavior with human proteins. In this study, an integrated computational approach combining molecular docking, molecular dynamics (MD) simulations, and in silico ADMET analysis was employed to investigate the interaction profile of creatinine with the human protein structure 7XTQ. Initial blind docking was performed using AutoDock Vina, followed by post-docking MD simulations to evaluate the structural stability and dynamic behavior of the protein-ligand complex. Docking results indicated weak surface-level interactions, which were further assessed through MD-derived parameters including proteins and ligand RMSD, RMSD, radius of gyration, and hydrogen bond analysis. MD simulations demonstrated overall structural stability of the protein and persistent proximity of creatinine at the protein surface without deep pocket insertion. ADMET predictions confirmed the biocompatible and non-toxic nature of creatinine. Collectively, these results suggest that creatinine exhibits weak, non-specific interactions with protein 7XTQ, providing insights into metabolite-protein surface recognition rather than therapeutic inhibition.