1. 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).
- Author
-
Ocampo-Hernández J, de Jesús Gómez-Guzmán J, Cruz-Ramírez M, Rebolledo-Chávez JPF, Mendoza A, Moreno-Esparza R, and Ortiz-Frade L
- Subjects
- Circular Dichroism, Spectrometry, Fluorescence, Copper chemistry, Serum Albumin, Bovine chemistry, Ethylenediamines
- 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 [CuΙΙ (Bztpen)]2+ +1e → [CuΙ (Bztpen)]+ and a weak interaction energy between BSA and [CuΙΙ (Bztpen)] and [CuΙ (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 [CuΙΙ (Bztpen)]2+ + 1e → [CuΙ (Bztpen)]+ . CD experiments at variable temperature for BSA denaturalization in the absence and in the presence of [CuΙΙ (Bztpen)]2+ , shown no change in thermodynamic parameters due to low interaction between the transport protein and copper complex., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier Inc. All rights reserved.)- Published
- 2022
- Full Text
- View/download PDF