Electrochemical and CD-spectroelectrochemical studies of the interaction between BSA and the complex [Cu(Bztpen)]2+, (Bztpen = (N-benzyl-N, N', N'-tris (pyridin-2-ylmethyl) ethylenediamine)

Abstract

In this work we report the electrochemical, spectroscopical and spectro-electrochemical studies of a model complex [Cu^ΙΙ(Bztpen)]²⁺, (Bztpen = (N-benzyl-N,N',N'-tris(pyridin-2-ylmethyl)ethylenediamine) in order to propose a methodology to evaluate the interaction of potential metal based anticancer agents during electron transfer processes, with transport proteins such as Bovine Serum Albumin (BSA). It was possible to establish a reversible electron transfer [Cu^ΙΙ(Bztpen)]²⁺ +1e → [Cu^Ι(Bztpen)]⁺ and a weak interaction energy between BSA and [Cu^ΙΙ(Bztpen)] and [Cu^Ι(Bztpen)] species, with no adsorption of protein over the electrode surface. Circular Dichroism (CD) Spectroelectrochemistry, not reported before, reveals no significant changes in BSA structure during the electron transfer [Cu^ΙΙ(Bztpen)]²⁺ + 1e → [Cu^Ι(Bztpen)]⁺. CD experiments at variable temperature for BSA denaturalization in the absence and in the presence of [Cu^ΙΙ(Bztpen)]²⁺, shown no change in thermodynamic parameters due to low interaction between the transport protein and copper complex.

Keywords: Circular dichroism; Copper complexes; Spectroelectrochemistry.