Comparative analysis of glimepiride interactions with bovine serum albumin and fibrinogen using fluorescence spectroscopy

¹ Department of Chemistry, University Institute of Sciences, Chandigarh University, Gharuan - 140413, Mohali, Punjab, India.
² Department of Chemistry, Research and Incubation Centre, Rayat Bahra University, Punjab India

^* Corresponding author: anuthakur2014@gmail.com

Abstract

Bovine Serum Albumin (BSA) and Fibrinogen (Fib) are the model proteins extensively used for investigating drug-protein interactions due to their distinct binding characteristics and structural similarities to human serum albumin. The present report examines the interactions between Glimepiride (GM) [a sulfonylurea used for Type 2 Diabetes mellitus management) and Fib And BSA, respectively. Fluorescence spectroscopy was employed to analyze quenching mechanisms and binding constants at 298 K and 290 K, respectively. The results indicate that GM binds to BSA and Fib via hydrophobic forces, with binding and quenching rate constants showing significant interactions. The binding constant (k_b) due to the interaction between GM-Fib was found to be 1.297 × 10⁴ Lmol^-1 and 1.262× 10⁴ Lmol^-1 at 298 K and 290 K, respectively with Gibbs free energy (ΔG) equal to -5.609 Kcal/mol, and -3.627 Kcal/mol at 298 K and 290 K, respectively. The binding constant (k_b) for the interaction between GM- BSA was determined to be 1.24 × 10⁵ Lmol⁻¹ at 298 K and 9.896 × 10³ Lmol⁻¹ at 290 K. The ΔG associated with these interactions is -6.947 Kcal/mol at 298 K and -5.302 Kcal/mol at 290 K. The thermodynamic parameters suggest spontaneous binding processes due to a negative value of ΔG. The results provide valuable insights into GM’s stability and interaction mechanisms with Fib and BSA, contributing to understanding drug-protein interactions essential for drug development.