DFT calculations of copper complexes mimicking superoxide dismutase and docking studies and molecular dynamics of the transition metal complex binding to serum albumin.

Superoxide dismutase (SOD) is a metalloenzyme whose antioxidant activity is mimicked by some transition metal complexes, and such ability can be added in proteins such as the bovine serum albumin (BSA), creating a hybrid protein. In this work, density functional theory (DFT) calculations of three Cu(II)-complexes of general formula [CuLphen] (phen = phenanthroline; , L = mefenamate; , L = tolfenamate; , L = flufenamate) with SOD-like activity, and docking and molecular dynamics (MD) simulations of these complexes with the BSA were performed. The DFT calculations revealed that the complex reduction involves Cu(II) → Cu(I) reduction, the theoretical electron affinity (EA) correlated with the SOD-like activity (IC), and the contribution of the phenanthroline ligand and the metal in LUMO it's related with the complex-protein interaction (K).

Electronic investigation of the effect of substituents on the SOD mimic activity of copper (II) complexes with 8-hydroxyquinoline-derived ligands.

Density functional theory (DFT) calculations were used to study the superoxide dismutase (SOD) mimic activity of two Cu complexes with ligands derived from 8-hydroxyquinoline (8-HQ). Electron-donating and -withdrawing substituent groups were inserted into the structures to verify changes in the reactivity. The theoretical parameters obtained were compared and validated with the experimental data available.