Published August 12, 2023 | Version v1
Journal article Open

A Review on Binding interactions between Anti-bacterial Drugs and Human serum albumin using fluorescence spectroscopy

Authors/Creators

  • 1. UGC

Description

Human serum albumin is a highly water soluble globular monomeric plasma protein with a relative
molecular weight of67 KDa. It hasthe centre of attention in the pharmaceutical industry due to their ability
to bind tovarious drug molecules. This review will address the properties of binding site of drugs in IIA
subdomain within the structure of HSA and also the mechanism of interaction of drugs with human serum
albumin has been studied using fluorescence spectroscopic technique. It Is allowed us to characterize the
strength and modes of binding, mechanism of fluorescence quenching, and intermolecular interactions for
the DRUG-HSA complexes. We determined that DRUG and HSA form two stable low-energy complexes,
leading to conformational changes and quenching of protein fluorescence. Stern–Volmer analysis of the
fluorescence also revealed a collision-independent static mechanism for fluorescence quenching upon
formation of the DRUG–HSA complex. The Stern –volmer analysis shown that the tryptophan residues of
albumin are not fully accessible to the dug and predominantly static mechanism is operative.

Notes

HSA is the most abundant protein in human blood plasma which constitutes about half of a serum protein and it is produced in the liver. In addition, HSA also transports hormones, fatty acids, unconjugated bilirubin and their compounds. It maintains oncotic pressure. Drug interaction with human serum albumin generally enhances the distribution and bioavailability of the drug depending on the specific pharmacokinetic properties of the drug molecules. Additionally, because of its abundance, human serum albumin plays a significant role in the pharmacokinetic behaviour of a variety of drugs, including: drug half-life in the bloodstream, decreasing drug toxicity, and improving drug targeting specificity. Fluorescence quenching of a substance by interaction with another, which is added in increasing amounts, can be used as a technique to measure the binding affinities between some macromolecules and ligands acting as suppressors (quenchers). A gradual decrease in the fluorescence emission intensity of HSA is observed in the presence of increasing concentrations of drug suggesting the presence of tryptophan residue of the HSA at or near the drug binding site. HSA has one Trp (Trp 214) and its fluorescence is solely due to the excitation of this residue of HSA located in the binding domain-IIA (site I) at the bottom. The quenching data was analysed using the Stern-Volmer equation:

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