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Binding Sites of Anticancer Drugs on Human Serum Albumin (HSA): A Review



Background:

To recognize the action of pharmacologically approved anticancer drugs in biological systems, information on its pharmacokinetics such as its transport within the plasma and delivery to its target site are 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 the circulation and plays a vital role in the efficacy, metabolism, distribution, and elimination of these agents.


Method:

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


Results:

the molecular docking reports were 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 anticancer drug complex binding.


Conclusion:

The results of this review study showed that site I of the protein located in domain 2 can be considered as the most important binding site for anticancer drugs.


Keywords:

Anticancer drug; Binding site; Fluorescence spectroscopy; Human serum albumin; Molecular docking; Neoplasm.



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