In-vitro Fluorescence Spectroscopic Analysis of the Interaction of Glimepiride with Bovine Serum Albumin (BSA)

Abstract

Background: The significant study was made to investigate the interaction of an antidiabetic drug, glimepiride with bovine serum albumin (BSA) by fluorescence quenching method in two different temperatures (298K and 308K).
 Methods: The study was carried out through fluorescence spectroscopic analysis. Stern-Volmer equation determined the fluorescence quenching constant. The various thermodynamic parameters such as free energy (ΔG), enthalpy (ΔH), and entropy (ΔS) was found out by Van’t Hoff equation.
 Results: The data revealed that glimepiride interact with BSA and both tryptophan and tyrosine residues of BSA are responsible for interactions with glimepiride. BSA undergo static quenching in presence of glimepiride, a quencher. The hydrophobic forces participated in chief roles for BSA-glimepiride complexation and this was indicated by the values of thermodynamic parameters. The binding number (n) obtained was ≈1 pointed out that glimepiride and BSA has bound with 1:1 ratio.
 Conclusions: Through fluorescence spectroscopic technique we revealed the nature of interaction of glimepiride with BSA, quenching mechanism for the interaction and associated thermodynamic parameters.

Insight into the interaction between tannin acid and bovine serum albumin from a spectroscopic and molecular docking perspective

“…This makes it easier to bind to active molecules and to form stable complexes with various endogenous and exogenous compounds such as ions, fatty acids, drug molecules and toxic exogenous compounds. 10,11 It has a transport function and is responsible for delivering endogenous or exogenous molecules to their targets. 12 The formation of high-affinity albumin-ligand complexes can inuence membrane transport, distribution and elimination of ligand molecules.…”