1. Comparative analysis of glimepiride interactions with bovine serum albumin and fibrinogen using fluorescence spectroscopy
- Author
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Pathania Apoorva, Deep Kour Harman, Bhattu Monika, and Radha Pathania Anu
- Subjects
Environmental sciences ,GE1-350 - 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 (kb) 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 (kb) 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.
- Published
- 2024
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