THERMODYNAMIC STUDY ON THE INTERACTION OF BIS(INDOLYL)METHANEDYE WITH HUMAN SERUM ALBUMIN

The interaction of bis(indolyl)methane (BIM) as one of the main active component of anticancer and antibacterial drugs, with human serum albumin (HSA), as drug carrier, was investigated at 293, 298, 303 and 310 K using Flu-orescence spectroscopy. Results revealed that the quenching mechanism for the interaction is static process. The results of quenching study used to calculate thermodynamic parameters which indicated that the binding process occurs spontaneously and demonstrated that human serum albumin provide very good binding via hydrogen bonds, Van der Waals forces and hydrophobic interactions. Fӧrster energy transfer measurements showed that BIM binds to the Trp residues of human serum albumin molecules in short distances.