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

doi:10.1016/j.aca.2008.11.070

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

Strathclyde Institute Of Pharmacy And Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

8 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.

Original language	English
Pages (from-to)	216-222
Number of pages	6
Journal	Analytica Chimica Acta
Volume	633
Issue number	2
DOIs	https://doi.org/10.1016/j.aca.2008.11.070
Publication status	Published - Feb 2009

Keywords

aldehyde
protein
adduct
fourier transform mass spectrometry
human plasma
pharmacology

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10.1016/j.aca.2008.11.070

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

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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author = "M. Pournamdari and Ahmed Saadi and E. Ellis and Ruth Andrew and Brian Walker and D.G. Watson",

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T1 - Development of a derivatisation method for the analysis of aldehyde modified amino acid residues in proteins by Fourier transform mass spectrometry

AU - Pournamdari, M.

AU - Saadi, Ahmed

AU - Ellis, E.

AU - Andrew, Ruth

AU - Walker, Brian

AU - Watson, D.G.

PY - 2009/2

Y1 - 2009/2

N2 - 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.

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

KW - protein

KW - adduct

KW - fourier transform mass spectrometry

KW - human plasma

KW - pharmacology

UR - http://dx.doi.org/10.1016/j.aca.2008.11.070

U2 - 10.1016/j.aca.2008.11.070

DO - 10.1016/j.aca.2008.11.070

M3 - Article

SN - 0003-2670

VL - 633

SP - 216

EP - 222

JO - Analytica Chimica Acta

JF - Analytica Chimica Acta

IS - 2

ER -

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

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Keywords

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