A new biomarker of protein oxidation degree and site using angiotensin as the target by MS

Spectrochim Acta A Mol Biomol Spectrosc. 2010 Feb;75(2):908-11. doi: 10.1016/j.saa.2009.12.034. Epub 2009 Dec 14.

Abstract

Hydroxyl radicals generated from Fenton reaction were used to damage the angiotensin. The oxidative damage degree and sites of peptides were measured by HPLC-MS and MS/MS. Experimental results proved that the oxidative damage degree increased with longer reaction time. The results also showed that the side chains of phenylalanine and tyrosine in angiotension can be attacked by hydroxyl radicals to form the oxidative products. A new strategy was established to monitor the oxidative degree and sites of peptides and laid the foundation for protein oxidation. This method can be used to investigate the mechanism of protein oxidative damage caused by oxidative stress which is induced by environmental pollutants and physiological activities. There will also be a wide application in the research of pathogenesis of some disease related to oxidative stress.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiotensins / chemistry*
  • Biomarkers / analysis*
  • Chromatography, High Pressure Liquid
  • Hydroxyl Radical*
  • Oxidation-Reduction
  • Oxidative Stress
  • Peptide Fragments / chemistry
  • Phenylalanine / chemistry
  • Proteins / chemistry*
  • Tandem Mass Spectrometry
  • Tyrosine / chemistry

Substances

  • Angiotensins
  • Biomarkers
  • Peptide Fragments
  • Proteins
  • Hydroxyl Radical
  • Tyrosine
  • Phenylalanine