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.
Highlights
Serum albumins are the most plenteous proteins in blood and it interacts with drugs to form drugprotein complexes [1]
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)
The data revealed that glimepiride interact with BSA and both tryptophan and tyrosine residues of BSA are responsible for interactions with glimepiride
Summary
Serum albumins are the most plenteous proteins in blood and it interacts with drugs to form drugprotein complexes [1]. Fluorescence spectroscopic method has been used due to its high sensitivity, relatively ease of use and reproducibility [10,11,12,13] to inspect the interaction of glimepiride with BSA molecule by calculating the participating amino acid residues, number of binding sites, thermodynamic parameters, fluorescence quenching rate constant and their binding constant. 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.
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