Abstract

Background: To recognize the action of pharmacologically approved anticancer drugs in biological systems, information regarding its pharmacokinetics, such as its transport within the plasma and delivery to its target site, is essential. In this study, we have tried to collect and present complete information about how these drugs bind to human serum albumin (HSA) protein. HSA functions as the main transport protein for an enormous variety of ligands in circulation and plays a vital role in the efficacy, metabolism, distribution, and elimination of these agents.

Methods: Therefore, this study includes information about the quenching constant, the binding constant obtained from Stern-Volmer and Hill equations, and molecular docking.

Results: Molecular docking was carried out to detect the binding models of HSA–anticancer drugs and the binding site of the drugs in HSA, which further revealed the contribution of amino acid residues of HSA in the drug complex binding.

Conclusion: This review study showed that site I of the protein located in domain II can be considered the most critical binding site for anticancer drugs.

Keywords: Human serum albumin, anticancer drug, neoplasm, molecular docking, binding site, fluorescence spectroscopy.