Sequencing of peptide‐derived Amadori products by the electron capture dissociation method

Stefanowicz, Piotr; Kijewska, Monika; Szewczuk, Zbigniew

doi:10.1002/jms.1580

Cited by 19 publications

(21 citation statements)

References 16 publications

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“…ECD performed on Fourier transform mass spectrometers was shown to be useful for the characterization of labile post-translational protein modification [22], including non-enzymatic modifications of basic side chains [11,23]. No fragmentation of phosphorylated histidine residues was observed during ECD experiments [24,25].…”

Section: Introductionmentioning

confidence: 99%

Electron capture dissociation mass spectrometric analysis of lysine-phosphorylated peptides

et al. 2010

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Phosphorylation of proteins is an essential signalling mechanism in eukaryotic and prokaryotic cells. Although N-phosphorylation of basic amino acid is known for its importance in biological systems, it is still poorly explored in terms of products and mechanisms. In the present study, two MS fragmentation methods, ECD (electron-capture dissociation) and CID (collision-induced dissociation), were tested as tools for analysis of N-phosphorylation of three model peptides, RKRSRAE, RKRARKE and PLSRTLSVAAKK. The peptides were phosphorylated by reaction with monopotassium phosphoramidate. The results were confirmed by 1H NMR and 31P NMR studies. The ECD method was found useful for the localization of phosphorylation sites in unstable lysine-phosphorylated peptides. Its main advantage is a significant reduction of the neutral losses related to the phosphoramidate moiety. Moreover, the results indicate that the ECD–MS may be useful for analysis of regioselectivity of the N-phosphorylation reaction. Stabilities of the obtained lysine-phosphorylated peptides under various conditions were also tested.

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Section: Introductionmentioning

confidence: 99%

Electron capture dissociation mass spectrometric analysis of lysine-phosphorylated peptides

et al. 2010

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“…Glycation of ubiquitin results in a mixture of isomeric compounds that differ by the number and location of glycated lysine moieties which was confirmed by analysis of the ECD fragmentation of synthetic peptide-derived Amadori products, thermally glycated ubiquitin as well as its peptide fragments [ 31 , 32 ].…”

Section: Resultsmentioning

confidence: 94%

The influence of glycation on a high pressure denaturation of ubiquitin

et al. 2016

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The combination of deuterium–hydrogen exchange (DHX) and mass spectrometry (MS) can be used for studying a high pressure denaturation (HPD) of proteins. Herein we present the results of investigations of the influence of glycation on the HPD of ubiquitin. Application of various values of pressure causes different degrees of protein unfolding, resulting in molecules with a different number of protons available for exchange with deuterons. The dependence of this number on pressure gives information on the denaturation state of a protein. On the basis of the obtained results we can conclude that increasing number of fructosamine moieties in ubiquitin decreases the pressure required for its denaturation. It suggests that glycation moderately decreases the protein stability. The present study is the first example of application of hydrogen–deuterium exchange as a method of investigating the influence of posttranslational modification of protein on the HPD.

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“…The glycation of ubiquitin followed by the enzymatic hydrolysis of the glycation product were performed according the procedures described previously [6]. …”

Section: Methodsmentioning

confidence: 99%

“…The abundance of peptide backbone fragments is relatively low and the sequence coverage is not sufficient to reconstruct the sequence of the studied peptide. Therefore, new techniques of ECD and ETD have been applied for the sequencing of the Amadori products [6, 7]. Another approach to the analysis of the primary structure of these compounds was based on a combination of enzymatic hydrolysis with mass spectrometry [8, 9].…”

Section: Introductionmentioning

confidence: 99%

Selective Detection of Carbohydrates and Their Peptide Conjugates by ESI-MS Using Synthetic Quaternary Ammonium Salt Derivatives of Phenylboronic Acids

Kijewska

Kuc

Kluczyk

et al. 2014

J. Am. Soc. Mass Spectrom.

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We present new tags based on the derivatives of phenylboronic acid and apply them for the selective detection of sugars and peptide-sugar conjugates in mass spectrometry. We investigated the binding of phenylboronic acid and its quaternary ammonium salt (QAS) derivatives to carbohydrates and peptide-derived Amadori products by HR-MS and MS/MS experiments. The formation of complexes between sugar or sugar-peptide conjugates and synthetic tags was confirmed on the basis of the unique isotopic distribution resulting from the presence of boron atom. Moreover, incorporation of a quaternary ammonium salt dramatically improved the efficiency of ionization in mass spectrometry. It was found that the formation of a complex with phenylboronic acid stabilizes the sugar moiety in glycated peptides, resulting in simplification of the fragmentation pattern of peptide-derived Amadori products. The obtained results suggest that derivatization of phenylboronic acid as QAS is a promising method for sensitive ESI-MS detection of carbohydrates and their conjugates formed by non-enzymatic glycation or glycosylation.FigureᅟElectronic supplementary materialThe online version of this article (doi:10.1007/s13361-014-0857-4) contains supplementary material, which is available to authorized users.

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Sequencing of peptide‐derived Amadori products by the electron capture dissociation method

Cited by 19 publications

References 16 publications

Electron capture dissociation mass spectrometric analysis of lysine-phosphorylated peptides

Electron capture dissociation mass spectrometric analysis of lysine-phosphorylated peptides

The influence of glycation on a high pressure denaturation of ubiquitin

Selective Detection of Carbohydrates and Their Peptide Conjugates by ESI-MS Using Synthetic Quaternary Ammonium Salt Derivatives of Phenylboronic Acids

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