CONFORMATIONAL CHANGE OF Α-CASEIN WITH INTERACTION OF BIS(INDOLYL)METHANE BY SPECTROSCOPIC AND MOLECULAR DOCKING TECHNIQUE

Spectroscopic and molecular docking techniques were used to study the interaction of bis(indolyl)methane, poorly soluble in aqueous solutions, with bovine α-casein nanoparticle, as an efficient drug carrier system. The results of FTIR and CD spectroscopy demonstrated that α-casein interacts with BIM molecule mainly via hydrophobic and hydrophilic interactions and changes secondary structure of α-casein. Synchronous fluorescence spectroscopy demonstrated the BIM most possible change the hydrophobicity around the Trp and Tyr residues of α-casein. The distance between donor and acceptor, obtained according to fluorescence resonance energy transfer (FRET) and docking studies, indicated that the BIM had hydrophobicity around the Trp residues of α-casein and transferred to an aqueous or hydrophilic environment.