A biotin enrichment strategy identifies novel carbonylated amino acids in proteins from human plasma

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

A biotin enrichment strategy identifies novel carbonylated amino acids in proteins from human plasma. / Havelund, Jesper F; Wojdyla, Katarzyna Iwona; Davies, Michael J; Jensen, Ole N.; Møller, Ian Max; Rogowska-Wrzesinska, Adelina.

In: Journal of Proteomics, Vol. 156, 06.03.2017, p. 40-51.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Havelund, JF, Wojdyla, KI, Davies, MJ, Jensen, ON, Møller, IM & Rogowska-Wrzesinska, A 2017, 'A biotin enrichment strategy identifies novel carbonylated amino acids in proteins from human plasma', Journal of Proteomics, vol. 156, pp. 40-51. https://doi.org/10.1016/j.jprot.2016.12.019

APA

Havelund, J. F., Wojdyla, K. I., Davies, M. J., Jensen, O. N., Møller, I. M., & Rogowska-Wrzesinska, A. (2017). A biotin enrichment strategy identifies novel carbonylated amino acids in proteins from human plasma. Journal of Proteomics, 156, 40-51. https://doi.org/10.1016/j.jprot.2016.12.019

Vancouver

Havelund JF, Wojdyla KI, Davies MJ, Jensen ON, Møller IM, Rogowska-Wrzesinska A. A biotin enrichment strategy identifies novel carbonylated amino acids in proteins from human plasma. Journal of Proteomics. 2017 Mar 6;156:40-51. https://doi.org/10.1016/j.jprot.2016.12.019

Author

Havelund, Jesper F ; Wojdyla, Katarzyna Iwona ; Davies, Michael J ; Jensen, Ole N. ; Møller, Ian Max ; Rogowska-Wrzesinska, Adelina. / A biotin enrichment strategy identifies novel carbonylated amino acids in proteins from human plasma. In: Journal of Proteomics. 2017 ; Vol. 156. pp. 40-51.

Bibtex

@article{170dd45da31b44b69d03273234c8ffc8,
title = "A biotin enrichment strategy identifies novel carbonylated amino acids in proteins from human plasma",
abstract = "Protein carbonylation is an irreversible protein oxidation correlated with oxidative stress, various diseases and ageing. Here we describe a peptide-centric approach for identification and characterisation of up to 14 different types of carbonylated amino acids in proteins. The modified residues are derivatised with biotin-hydrazide, enriched and characterised by tandem mass spectrometry. The strength of the method lies in an improved elution of biotinylated peptides from monomeric avidin resin using hot water (95°C) and increased sensitivity achieved by reduction of analyte losses during sample preparation and chromatography. For the first time MS/MS data analysis utilising diagnostic biotin fragment ions is used to pinpoint sites of biotin labelling and improve the confidence of carbonyl peptide assignments. We identified a total of 125 carbonylated residues in bovine serum albumin after extensive in vitro metal ion-catalysed oxidation. Furthermore, we assigned 133 carbonylated sites in 36 proteins in native human plasma protein samples. The optimised workflow enabled detection of 10 hitherto undetected types of carbonylated amino acids in proteins: aldehyde and ketone modifications of leucine, valine, alanine, isoleucine, glutamine, lysine and glutamic acid (+14Da), an oxidised form of methionine - aspartate semialdehyde (-32Da) - and decarboxylated glutamic acid and aspartic acid (-30Da).BIOLOGICAL SIGNIFICANCE: Proteomic tools provide a promising way to decode disease mechanisms at the protein level and help to understand how carbonylation affects protein structure and function. The challenge for future research is to identify the type and nature of oxidised residues to gain a deeper understanding of the mechanism(s) governing carbonylation in cells and organisms and assess their role in disease.",
keywords = "Journal Article",
author = "Havelund, {Jesper F} and Wojdyla, {Katarzyna Iwona} and Davies, {Michael J} and Jensen, {Ole N.} and M{\o}ller, {Ian Max} and Adelina Rogowska-Wrzesinska",
note = "Copyright {\circledC} 2017 Elsevier B.V. All rights reserved.",
year = "2017",
month = "3",
day = "6",
doi = "10.1016/j.jprot.2016.12.019",
language = "English",
volume = "156",
pages = "40--51",
journal = "Journal of Proteomics",
issn = "1874-3919",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - A biotin enrichment strategy identifies novel carbonylated amino acids in proteins from human plasma

AU - Havelund, Jesper F

AU - Wojdyla, Katarzyna Iwona

AU - Davies, Michael J

AU - Jensen, Ole N.

AU - Møller, Ian Max

AU - Rogowska-Wrzesinska, Adelina

N1 - Copyright © 2017 Elsevier B.V. All rights reserved.

PY - 2017/3/6

Y1 - 2017/3/6

N2 - Protein carbonylation is an irreversible protein oxidation correlated with oxidative stress, various diseases and ageing. Here we describe a peptide-centric approach for identification and characterisation of up to 14 different types of carbonylated amino acids in proteins. The modified residues are derivatised with biotin-hydrazide, enriched and characterised by tandem mass spectrometry. The strength of the method lies in an improved elution of biotinylated peptides from monomeric avidin resin using hot water (95°C) and increased sensitivity achieved by reduction of analyte losses during sample preparation and chromatography. For the first time MS/MS data analysis utilising diagnostic biotin fragment ions is used to pinpoint sites of biotin labelling and improve the confidence of carbonyl peptide assignments. We identified a total of 125 carbonylated residues in bovine serum albumin after extensive in vitro metal ion-catalysed oxidation. Furthermore, we assigned 133 carbonylated sites in 36 proteins in native human plasma protein samples. The optimised workflow enabled detection of 10 hitherto undetected types of carbonylated amino acids in proteins: aldehyde and ketone modifications of leucine, valine, alanine, isoleucine, glutamine, lysine and glutamic acid (+14Da), an oxidised form of methionine - aspartate semialdehyde (-32Da) - and decarboxylated glutamic acid and aspartic acid (-30Da).BIOLOGICAL SIGNIFICANCE: Proteomic tools provide a promising way to decode disease mechanisms at the protein level and help to understand how carbonylation affects protein structure and function. The challenge for future research is to identify the type and nature of oxidised residues to gain a deeper understanding of the mechanism(s) governing carbonylation in cells and organisms and assess their role in disease.

AB - Protein carbonylation is an irreversible protein oxidation correlated with oxidative stress, various diseases and ageing. Here we describe a peptide-centric approach for identification and characterisation of up to 14 different types of carbonylated amino acids in proteins. The modified residues are derivatised with biotin-hydrazide, enriched and characterised by tandem mass spectrometry. The strength of the method lies in an improved elution of biotinylated peptides from monomeric avidin resin using hot water (95°C) and increased sensitivity achieved by reduction of analyte losses during sample preparation and chromatography. For the first time MS/MS data analysis utilising diagnostic biotin fragment ions is used to pinpoint sites of biotin labelling and improve the confidence of carbonyl peptide assignments. We identified a total of 125 carbonylated residues in bovine serum albumin after extensive in vitro metal ion-catalysed oxidation. Furthermore, we assigned 133 carbonylated sites in 36 proteins in native human plasma protein samples. The optimised workflow enabled detection of 10 hitherto undetected types of carbonylated amino acids in proteins: aldehyde and ketone modifications of leucine, valine, alanine, isoleucine, glutamine, lysine and glutamic acid (+14Da), an oxidised form of methionine - aspartate semialdehyde (-32Da) - and decarboxylated glutamic acid and aspartic acid (-30Da).BIOLOGICAL SIGNIFICANCE: Proteomic tools provide a promising way to decode disease mechanisms at the protein level and help to understand how carbonylation affects protein structure and function. The challenge for future research is to identify the type and nature of oxidised residues to gain a deeper understanding of the mechanism(s) governing carbonylation in cells and organisms and assess their role in disease.

KW - Journal Article

U2 - 10.1016/j.jprot.2016.12.019

DO - 10.1016/j.jprot.2016.12.019

M3 - Journal article

C2 - 28062376

VL - 156

SP - 40

EP - 51

JO - Journal of Proteomics

JF - Journal of Proteomics

SN - 1874-3919

ER -

ID: 182331313