Abstract

FLUORESCENCE SPECTROSCOPIC ANALYSIS OF THE INTERACTION BETWEEN OMEPRAZOLE AND BOVINE SERUM ALBUMIN

Kanij Nahar Deepa*, Shaila Kabir and Md. Shah Amran

ABSTRACT

The interaction between drug molecule and protein may result in the formation of stable protein-drug complex having influence on the pharmacokinetics of a drug. In the present study, the mutual interaction of Omeprazole with bovine serum albumin (BSA) was investigated using fluorescence spectroscopy under different conditions. It was observed that the fluorescence quenching by Omeprazole was a result of static quenching, that is, the formation of Omeprazole-BSA complex at excited state with probable involvement of tryptophan residue. Fluorescence quenching constants were determined using the Stern-Volmer equation. The thermodynamic parameters such as Gibb’s free energy (ΔG), enthalpy change (ΔH), and entropy change (ΔS) at different temperatures were studied by using van’t Hoff equation. The values of ΔG, ΔH and ΔS at 298K were found -31.58 KJ/mol, -78.66 KJ/mol and -157.97 J/mol for Omeprazole. The binding of Omeprazole to BSA was found spontaneous and endothermic where van der Waals forces and hydrogen bond playing a major role in the Omeprazole-BSA binding.

Keywords: Stern-Volmer, Omeprazole-BSA.