Bovine Serum Albumin Metal Complexes for Mimic of SOD

Abstract

Superoxide anion radical (O$_{2}^{\bullet -}$) is a noxious reactive oxygen species (ROS). Transition metal ion complexes have been generally used as antioxidants to eliminate ROS. In this work, a neoteric water-soluble biopolymer metal complex (BSA-M) was prepared by conjugating the soluble biopolymer bovine serum albumin (BSA) with three transition metal ions (M, M =Cu, Co, Mn). The binding mode and ratio of metal ions bound to albumin were investigated. The BSA-M complexes were characterized by UV-Vis, circular dichroism (CD) spectra and polyacrylamide gel electrophoresis (PAGE). BSA served as polymer scaffold and the metal complex functioned as the catalytic active center. The results demonstrated that the structure of BSA remained unchanged when the binding ratio of transition metal ion complex to BSA was 5:1. Furthermore, the scavenging superoxide anion free radical (O$_{2}^{\bullet -}$) activity of biopolymer-metal complexes were determined by nitroblue tetrazolium light reduction assay method. The antioxidant capacity of BSA-M has markedly increased. The conjugated BSA-M (M=Cu, Mn) showed preeminent scavenging activity for O$_{2}^{\bullet -}$, and the EC₅₀ value of the BSA-Cu was 0.038 ±0.0013 μ mol⋅L ⁻¹, which is comparable to EC₅₀ value (0.041±0.001 μ mol⋅L ⁻¹) of the natural superoxide dismutase (SOD), the analog quantity reached 107%. As a consequence, it can be considered as a bio-functional mimic of enzyme SOD and has a promising application prospect in antioxidant drug field.