Interaction of gallium, indium and vanadyl diacetylcurcumin complexes with lysozyme: mechanistic aspects and evaluation of antiamyloidogenic activity.

Diacetylcurcumin as a derivative of curcumin is a strong nitric oxide (NO) and Oanion scavenger. One strategy to improve stability of curcumin and its derivatives is complexation with metal. In this study, the binding interactions of gallium diacetylcurcumin (Ga(DAC)), indium diacetylcurcumin (In(DAC)), and vanadyl diacetylcurcumin (VO(DAC)) with hen egg white lysozyme (HEWL) have been investigated. The results of fluorescence quenching analyses revealed that In(DAC) and VO(DAC) have higher binding affinities than Ga(DAC) towards HEWL. The interactions of these metal complexes were not accompanied by considerable conformational changes in the tertiary structure of HEWL. Furthermore, the inhibitory effects of these complexes on the amyloid fibrillation of HEWL were confirmed by the thioflavin T fluorescence assays. The kinetic curves of the fibrillation process illustrated that VO(DAC) has the highest inhibitory activity and In(DAC) has a significant delaying effect on the formation of amyloid fibrils of HEWL.