Structure, enzymatic activities, glycation and therapeutic potential of human serum albumin: A natural cargo

Abstract

Human serum albumin (HSA) is an opulent, non-glycosylated, most versatile carrier protein in plasma possessing multiple functions. HSA has the ability to interact with a variety of ligands, including exogenous pharmacological drugs. HSA has multiple binding sites located in different subdomains and which are responsible for binding of ligands. While antecedent research has discovered various functional and structural properties of HSA, the objective of this review paper is to shed light on some of the important properties of HSA and how binding pattern of different ligands can sustain the development of new drugs. Some significant properties include transportation, ligand-binding, distribution and metabolism of a compound. The HSA molecule can undergo various structural changes modifying its conformation and finally affects the ligand binding properties and redox state. Another important feature is an esterase-like activity possessed by HSA, which is also crucial in converting the prodrugs into active therapeutics. Therefore, HSA is one of the most suitable molecules for future research in drug discovery in pharmaceutical industry because of its numerous features and binding pattern that also governs the metabolism and drug dosage.