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 journalArticle

6 Citations (Scopus)

Abstract

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.
LanguageEnglish
Pages216-222
Number of pages6
JournalAnalytica Chimica Acta
Volume633
Issue number2
DOIs
Publication statusPublished - Feb 2009

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Fourier Analysis
aldehyde
Aldehydes
Fourier transform
Lysine
Mass spectrometry
serum
Mass Spectrometry
Fourier transforms
amino acid
mass spectrometry
Bovine Serum Albumin
Amino Acids
protein
Plasma (human)
liquid chromatography
hydrolysis
Proteins
Liquid chromatography
Reaction products

Keywords

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

Cite this

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abstract = "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.",
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Development of a derivatisation method for the analysis of aldehyde modified amino acid residues in proteins by Fourier transform mass spectrometry. / Pournamdari, M.; Saadi, Ahmed; Ellis, E.; Andrew, Ruth; Walker, Brian; Watson, D.G.

In: Analytica Chimica Acta, Vol. 633, No. 2, 02.2009, p. 216-222.

Research output: Contribution to journalArticle

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AU - Pournamdari, M.

AU - Saadi, Ahmed

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AU - Andrew, Ruth

AU - Walker, Brian

AU - Watson, D.G.

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AB - 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.

KW - aldehyde

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KW - adduct

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KW - human plasma

KW - pharmacology

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