Development of a derivatisation method for the analysis of aldehyde modified amino acid residues in proteins by Fourier transform mass spectrometry

M. Pournamdari, Ahmed Saadi, E. Ellis, Ruth Andrew, Brian Walker, D.G. Watson

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


A method was developed for the analysis of amino acids within bovine serum albumin (BSA) which had been modified by reaction with different enals. BSA was reacted with the aldehydes and the reaction products were stabilised by reaction with NaBH4. The protein was then hydrolysed with 6N HCl and the hydrolysis products were analysed by liquid chromatography-mass spectrometry (LC-MS). The modified amino acids were derivatised with propylchloroformate. High resolution mass spectrometry carried out using an LTQ-Orbitrap instrument which was able to characterise a wide range of adducts. In addition double adducts were observed to be formed with 4-hydroxynonenal (HNE) and lysine or lysine + histidine. Qualitatively it was possible to consistently observe a pyridinium adduct formed between lysine and pentenal in human plasma from normal subjects.
Original languageEnglish
Pages (from-to)216-222
Number of pages6
JournalAnalytica Chimica Acta
Issue number2
Publication statusPublished - Feb 2009


  • aldehyde
  • protein
  • adduct
  • fourier transform mass spectrometry
  • human plasma
  • pharmacology

Cite this