2-Methylaminopyridine-copper (II) complex catalyzes protein degradation.

Abstract

To investigate the mechanism of scission of proteins by the chemical cleaving agents like metal complexes, bovine serum albumin (BSA) has been treated by the copper(II) complex CuL2SO4, where L is 2-methylaminopyridine. BSA degradation increased with increasing the concentration of the copper complex. Copper complex rapidly degraded BSA at mild acidic and neutral pH values while no degradation occurred at alkaline pH values. Moreover, the degradation was increased at higher temperatures. Copper complex act as a catalyst for the polypeptide hydrolysis. The protein degradation was protected with beta-mercaptoethanol by acting as radical scavenger. H2O2 increased BSA degradation which is apparent by the disappearance of the original band. H2O2 reacts with copper complex to produce a reactive oxygen species (ROS), such as hydroxyl radical or a metal-coordinated oxo or peroxo species, which in turn can initiate cleavage of the peptide backbone nearby.