Abstract

SPECTROSCOPIC AND ELECTROCHEMICAL INVESTIGATION OF BINDING OF NEVIRAPINE WITH BOVINE SERUM ALBUMIN

M.M.V. Ramana*, Rahul Betkar, Amey Nimkar, Prasanna Ranade, Balaji Mundhe

Abstract

Nevirapine is a non-nucleoside reverse transcriptase inhibitor used for the treatment of Human Immunodeficiency Virus Type-1 infection and AIDS. A systematic interaction between nevirapine and bovine serum albumin (BSA) has been investigated by UV-Vis absorption, infra-red (IR) spectra, fluorescence, circular dichroism (CD), cyclic voltammetry (CV), and nuclear magnetic resonance (NMR) spectroscopy. UV-Vis absorption and fluorescence quenching is attributed to the formation of nevirapine-BSA complex. The fluorescence analysis indicates the quenching of BSA by nevirapine occurs through static procedure. Synchronous fluorescence, CD, and IR spectra revealed the conformation and microenvironment of BSA were altered by interaction with nevirapine. NMR spectroscopic results suggested hydrogen bonding and hydrophobic interactions played an important role in nevirapine-BSA complex formation. Cyclic voltammetry (CV) proved the interaction of nevirapine with BSA forming an electrochemically inactive complex.

Keywords: BSA, nevirapine, fluorescence quenching, circular dichroism, cyclic voltammetry, NMR.