Use of narrow mass-window, high-resolution extracted product ion chromatograms for the sensitive and selective identification of protein modifications

Corinne M. Spickett, Ana Reis, Andrew R. Pitt*

*Corresponding author for this work

Research output: Contribution to journalArticle

Abstract

Protein modifications, including oxidative modifications, glycosylations, and oxidized lipid-protein adducts, are becoming increasingly important as biomarkers and in understanding disease etiology. There has been a great deal of interest in mapping these on Apo B100 from low density lipoprotein (LDL). We have used extracted ion chromatograms of product ions generated using a very narrow mass window from high-resolution tandem mass spectrometric data collected on a rapid scanning quadrupole time-of-flight (QTOF) instrument, to selectively and sensitively detect modified peptides and identify the site and nature of a number of protein modifications in parallel. We have demonstrated the utility of this method by characterizing for the first time oxidized phospholipid adducts to LDL and human serum albumin and for the detection of glycosylation and kynurenin formation from the oxidation of tryptophan residues in LDL.

Original languageEnglish
Pages (from-to)4621-4627
Number of pages7
JournalAnalytical Chemistry
Volume85
Issue number9
Early online date27 Mar 2013
DOIs
Publication statusPublished - 7 May 2013

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LDL Lipoproteins
Glycosylation
Ions
Proteins
Biomarkers
Serum Albumin
Tryptophan
Phospholipids
Scanning
Lipids
Oxidation
Peptides

Bibliographical note

Funding: Engineering and Physical Sciences Research Council (EPSRC), UK [EP/I017887/1]; European Union FP7 PEOPLE Programme; Marie-Curie Intra-European Fellowship (FP7-PEOPLE-2009-IEF Project [255076]

Cite this

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title = "Use of narrow mass-window, high-resolution extracted product ion chromatograms for the sensitive and selective identification of protein modifications",
abstract = "Protein modifications, including oxidative modifications, glycosylations, and oxidized lipid-protein adducts, are becoming increasingly important as biomarkers and in understanding disease etiology. There has been a great deal of interest in mapping these on Apo B100 from low density lipoprotein (LDL). We have used extracted ion chromatograms of product ions generated using a very narrow mass window from high-resolution tandem mass spectrometric data collected on a rapid scanning quadrupole time-of-flight (QTOF) instrument, to selectively and sensitively detect modified peptides and identify the site and nature of a number of protein modifications in parallel. We have demonstrated the utility of this method by characterizing for the first time oxidized phospholipid adducts to LDL and human serum albumin and for the detection of glycosylation and kynurenin formation from the oxidation of tryptophan residues in LDL.",
author = "Spickett, {Corinne M.} and Ana Reis and Pitt, {Andrew R.}",
note = "Funding: Engineering and Physical Sciences Research Council (EPSRC), UK [EP/I017887/1]; European Union FP7 PEOPLE Programme; Marie-Curie Intra-European Fellowship (FP7-PEOPLE-2009-IEF Project [255076]",
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AU - Spickett, Corinne M.

AU - Reis, Ana

AU - Pitt, Andrew R.

N1 - Funding: Engineering and Physical Sciences Research Council (EPSRC), UK [EP/I017887/1]; European Union FP7 PEOPLE Programme; Marie-Curie Intra-European Fellowship (FP7-PEOPLE-2009-IEF Project [255076]

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