Exploring the interaction of naringenin with bovine beta-casein nanoparticles using spectroscopy

Abstract

Casein is composed of four types of protein α s1, α s2, β and ƙ in ratios of 4:1:4:1. β-casein has a lower critical micelle concentration than the other three types which results in its higher stability in the aqueous medium. The self-assembly, the unique feature of β-casein, helps to form the micelles without the need to emulsifiers and stabilizers, which they may have some adverse effects on the body. Naringenin is the main flavone in grapefruit that has several pharmacological properties such as antioxidant, anticancer and anti-inflammatory effects. Since naringenin is hydrophobic, its solubility in water could be raised by β-casein. In this study, the binding of naringenin with bovine β-casein is investigated at neutral pH 7.0. For this purpose, fluorescence spectroscopy technique was used. By using fluorescence quenching methods, the Stern–Volmer quenching constant (KSV), the number of binding sites (n), binding constants (Kb) and thermodynamic parameters ΔH, ΔG and ΔS were calculated at 298, 303 and 308 K. For estimating the distance between donor (β-casein) and acceptor (naringenin), fluorescence resonance energy transfer was used.