Ligand binding strategies of human serum albumin: How can the cargo be utilized?

2009/03/24 by Ankita Varshney, Priyankar Sen, Ejaz Ahmad +4 · 2 citations
Biochemistry, Genetics and Molecular Biology · Medicine · #Drug Transport and Resistance Mechanisms #Protein Interaction Studies and Fluorescence Analysis #Protein purification and stability

paper · pdf · doi:10.1002/chir.20709

openalex publication_date 2009/03/24 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/29

Abstract

Human serum albumin (HSA), being the most abundant carrier protein in blood and a modern day clinical tool for drug delivery, attracts high attention among biologists. Hence, its unfolding/refolding strategies and exogenous/endogenous ligand binding preference are of immense use in therapeutics and clinical biochemistry. Among its fellow proteins albumin is known to carry almost every small molecule. Thus, it is a potential contender for being a molecular cargo/or nanovehicle for clinical, biophysical and industrial purposes. Nonetheless, its structure and function are largely regulated by various chemical and physical factors to accommodate HSA to its functional purpose. This multifunctional protein also possesses enzymatic properties which may be used to convert prodrugs to active therapeutics. This review aims to highlight current overview on the binding strategies of protein to various ligands that may be expected to lead to significant clinical applications.

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