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  HCD Fragmentation of Glycated Peptides

Keilhauer, E. C., Geyer, P. E., & Mann, M. (2016). HCD Fragmentation of Glycated Peptides. Journal of Proteome Research, 15(8), 2881-2890. doi:10.1021/acs.jproteome.6b00464.

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 Creators:
Keilhauer, Eva C.1, Author              
Geyer, Philipp E.1, Author              
Mann, Matthias1, Author              
Affiliations:
1Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Free keywords: DISSOCIATION MASS-SPECTROMETRY; HUMAN PLASMA PROTEOME; DIABETES-MELLITUS; NONENZYMATIC GLYCOSYLATION; QUANTITATIVE-ANALYSIS; HEMOGLOBIN-A; PROTEINS; ENDPRODUCTS; IDENTIFICATION; COMPLICATIONSBiochemistry & Molecular Biology; protein glycation; higher-energy collisional dissociation; diabetes; blood plasma; AGEs;
 Abstract: Protein glycation is a concentration-dependent nonenzymatic reaction of reducing sugars with amine groups of proteins to form early as well as advanced glycation (end-) products (AGEs). Glycation is a highly disease-relevant modification but is typically only studied on a few blood proteins. To complement our blood proteomics studies in diabetics, we here investigate protein glycation by higher energy collisional dissociation (HCD) fragmentation on Orbitrap mass spectrometers. We established parameters to most efficiently fragment and identify early glycation products on in vitro glycated model proteins. Retaining standard collision energies does not degrade performance if the most dominant neutral loss of H6O3 is included into the database search strategy. Glycation, analysis of the entire HeLa proteome revealed an unexpected intracellular preponderance for arginine over lysine modification in early and advanced glycation (end-) products. Single-run analysis from 1 mu L of undepleted and unenriched blood plasma identified 101 early glycation sites as well as numerous AGE sites on diverse plasma proteins. We conclude that HCD fragmentation is well-suited for analyzing glycated peptides and that the diabetic status of patients can be directly diagnosed from single-run plasma proteomics measurements.

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Language(s): eng - English
 Dates: 2016-07-182016-08-05
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
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Title: Journal of Proteome Research
  Other : J. Proteome Res.
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Chemical Society
Pages: - Volume / Issue: 15 (8) Sequence Number: - Start / End Page: 2881 - 2890 Identifier: ISSN: 1535-3893
CoNE: https://pure.mpg.de/cone/journals/resource/111019664290000