In-vitro Fluorescence Spectroscopic Analysis of the Interaction of Glimepiride with Bovine Serum Albumin (BSA)
Kanij Nahar Deepa
Department of Pharmacy, University of Asia Pacific, Dhaka 1215, Bangladesh and Department of Pharmaceutical Chemistry, Faculty of Pharmacy, University of Dhaka, Dhaka-1000, Bangladesh.
Sabia Nawsheen
Department of Pharmacy, University of Asia Pacific, Dhaka 1215, Bangladesh.
Md. Abu Sufian
Department of Pharmacy, University of Asia Pacific, Dhaka 1215, Bangladesh.
S. M. Ashraful Islam *
Department of Pharmacy, University of Asia Pacific, Dhaka 1215, Bangladesh.
*Author to whom correspondence should be addressed.
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.
Keywords: Glimepiride, bovine serum albumin, fluorescence spectroscopy, drug-protein binding, thermodynamic parameter, quenching.