THERMODYNAMIC STUDY ON THE INTERACTION OF BOVINE MILK α-CASEIN WITH DIPYRIDAMOLE DRUG

Dipyridamole (DIP) is a coronary vasodilator and used as a coactivator of antitumor compounds poorly soluble in aqueous solutions. The interaction of bovine milk α-casein as an efficient drug carrier system with DIP was investigated using fluorescence methods. The fluorescence quenching measurements revealed the presence of a single binding site on α-casein for DIP with a binding constant of about 104 M-1. The quenching mechanism is static process and the negative free binding energy indicated the spontaneity of the binding processes of α-casein with DIP molecule. However, other thermodynamic parameters including and demonstrated that α-casein provide very good binding and entrapment to DIP via hydrogen bonds and Van der Waals forces.