Study on the interaction of silver(I) complex with bovine serum albumin by spectroscopic techniques

The interaction of silver(I) complex, [Ag (2,9-dimethyl-1,10-phenanthroline)(2)](NO3)center dot H2O, and bovine serum albumin (BSA) was investigated by spectrophotometry, spectrofluorimetry and circular dichroism (CD) techniques. The experimental results indicated that the quenching mechanism of BSA by the complex was a static procedure. Various binding parameters were evaluated. The negative value of Delta H, negative value of Delta S and the negative value of Delta G indicated that van der Waals force and hydrogen bonding play major roles in the binding of the complex and BSA. Based on Forster's theory of non-radiation energy transfer, the binding distance, r, between the donor (BSA) and acceptor (Ag(I) complex) was evaluated. The results of CD and UV-vis spectroscopy showed that the binding of this complex could bind to BSA and be effectively transported and eliminated in the body. (C) 2012 Elsevier B.V. All rights reserved.