Characterize the interaction between naringenin and bovine serum albumin using spectroscopic approach

Abstract

Naringenin, a flavanone compound highly enriched in grapefruits, has been identified as a possible inhibitor of cell proliferation; and thus has the potential to act as an antitumorigenic agent. In this study, the binding of naringenin to bovine serum albumin (BSA) was studied at the physiological conditions (pH=7.40) by fluorescence and UV–vis spectroscopy. Naringenin strongly quenches the intrinsic fluorescence of BSA, and a decrease in the fluorescence quenching constant was observed together with an increase in temperature, which indicates that the fluorescence quenching of BSA by naringenin is a result of the formation of naringenin–BSA complex. Binding parameters calculating from Stern-Volmer method and Scatchard method showed that naringenin bind to BSA with the binding affinities of the order 10 4 L mol −1. Thermodynamic parameters such as Δ G, Δ H and Δ S, were calculated at different temperatures, showing that electrostatic interactions were mostly responsible for the binding of naringenin to BSA. Site marker competitive displacement experiments demonstrating that naringenin bind with high affinity to site I (subdomain IIA) of BSA. Furthermore, the effect of metal ions to naringenin–BSA system was studied, and the specific binding distance r (3.30 nm) between donor (Trp-212) and acceptor (naringenin) was obtained according to fluorescence resonance energy transfer (FRET).