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)·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 ΔH, negative value of ΔS and the negative value of ΔG 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.

In this study, an attempt has been made to study the interaction of a silver(I) complex with the transport proteins, bovine serum albumin (BSA) employing UV–vis, fluorometric and circular dichroism (CD) techniques.Figure optionsDownload as PowerPoint slideHighlights
► Silver is a metal of interest in cancer therapy because its toxicity is quite low.
► The interaction between BSA metal–phenanthroline complexes has attracted great interest.
► The pharmaceutical design problems are avoiding precipitation of silver(I) by complexation.