From in silico docking to in vivo relevance: Predicting drug binding to ligand-bound human serum albumin

Title : From in silico docking to in vivo relevance: Predicting drug binding to ligand-bound human serum albumin

Abstract:

Binding of drugs to plasma proteins plays a critical role in determining pharmacokinetics, bioavailability, and therapeutic efficacy. Among plasma proteins, Human Serum Albumin is the primary carrier responsible for transporting a wide range of endogenous compounds and pharmaceutical agents in circulation. However, in vivo conditions often involve albumin already bound to endogenous ligands such as fatty acids, bilirubin, or other drugs, which can alter the availability and affinity of binding sites. This lecture explores the application of molecular docking as a computational tool to predict drug binding behavior in ligand-occupied albumin systems. By modeling drug interactions with ligand-bound conformations of human serum albumin, docking studies can provide insights into competitive binding, site displacement, and potential drug–drug interactions. Such in silico approaches offer a rapid and cost-effective strategy to complement experimental binding studies and improve the prediction of pharmacologically relevant interactions. Integrating molecular docking with pharmacokinetic knowledge can enhance our understanding of drug distribution under physiologically realistic conditions.

Biography:

Dr. Saad Tayyab studied Biochemistry at Aligarh Muslim University, India, completing Masters and Ph.D. degrees in 1981 and 1987, respectively. He is currently working as a Professor of Pharmaceutical Chemistry at UCSI University, Kuala Lumpur, Malaysia. Before joining UCSI University, Dr. Saad served at Universiti Malaya (2004-2018), Haramaya University, Ethiopia (2001-2004), Aligarh Muslim University, India (1988-2001), and the University of Kashmir, India (1987-1988). He was admitted as a Fellow, Royal Society of Chemistry, UK, in 2017, Fellow, Royal Society of Biology, UK, in 2019, Member, American Chemical Society in 2020, and Member, Sigma Xi in 2024. He is serving as an Editorial Board member for several journals. He has published over 150 journal papers, 17 popular articles, 1 book, 2 book chapters, and 1 learning aid. Several research students (16 Ph.D., 6 M.Phil., 1 M.D., and 13 M.Sc.) completed their degrees under his supervision, and he guided 32 undergraduate projects. His research interests include drug-protein interaction, protein folding, protein/enzyme stability, and protein structure-function. He possesses an h-index of 27, and his name is included in the reviewers’ lists of many international journals.