Bovine β-casein binding studies of a Schiff base ligand: fluorescence and circular dichroism approaches

In this study, a Schiff base derived from a heterocyclic moiety was synthesized and characterized. The in vitro binding behaviour of this ligand with β-casein (β-CN) was investigated using biophysical techniques. For evaluation, thermodynamics variables of interactions between the Schiff base ligand and β-CN, such as fluorescence at different temperatures, were measured. The results showed that the Schiff base ligand possessed considerable associated binding to β-CN and that the procedure was enthalpy driven. The β-CN conformation was also changed to give a further unfolded structure. Fluorescence resonance energy transfer was used to estimate the interval between donor (β-CN) and acceptor (Schiff base ligand). All these experimental results proposed that β-CN might act as carrier protein for the Schiff base ligand to deliver it to the target molecules.