Surface-enhanced Raman spectral features enrichment by selective hydrolysis of protein molecule peptide bonds

Abstract

The possibilities of surface-enhanced Raman spectral features enrichment by selective hydrolysis of protein molecule peptide bonds were investigated using fibrinogen oxidative modification with hypochlorite as an example. Enzymatic hydrolysis of native and oxidant-treated fibrinogen enables detection of vibrational bands related to the oxidation products of the amino acid residue side chains, mostly of methionine and tryptophan ones. The obtained data were confirmed by HPLC-MS/MS. These findings open up possibilities for the exploitation of the proposed approach as a tool in protein oxidative modification research.