Fragmentation behavior of glycated peptides derived from <scp>D</scp>‐glucose, <scp>D</scp>‐fructose and <scp>D</scp>‐ribose in tandem mass spectrometry

Frolov, Andrej; Hoffmann, Peter; Hoffmann, Ralf

doi:10.1002/jms.1117

Cited by 101 publications

(121 citation statements)

References 32 publications

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“…Furthermore, the loss of the sugar moiety together with the amine group, which was predominant in the above-mentioned forms of CSF114, is completely absent here, probably because it could generate an unstable primary carbocation on the residual group of the lysine. The spectrum is dominated by the cleavages inside the sugar moiety and b-ions are very weak or even absent, as previously reported; [38] consequently, it is very difficult to obtain sequence information from this spectrum. For this reason, MS 3 fragmentation was used to have a better sequence coverage for the peptide.…”

Section: Sugar-peptide Analogs Of Csf114supporting

confidence: 55%

Multi-Stage Mass Spectrometry Analysis of Sugar-Conjugated β-Turn Structures to be Used as Probes in Autoimmune Diseases

Gentilini

Auberger

Rentier

et al. 2016

J. Am. Soc. Mass Spectrom.

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Abstract. Synthetic sugar-modified peptides were identified as antigenic probes in the context of autoimmune diseases. The aim of this work is to provide a mechanistic study on the fragmentation of different glycosylated analogs of a synthetic antigenic probe able to detect antibodies in a subpopulation of multiple sclerosis patients. In particular the N-glucosylated type I′ β-turn peptide structure called CSF114(Glc) was used as a model to find signature fragmentations exploring the potential of multistage mass spectrometry by MALDI-LTQ Orbitrap. Here we compare the fragmentation of the glucosylated form of the synthetic peptide CSF114(Glc), bearing a glucose moiety on an asparagine residue, with less or non-immunoreactive forms, bearing different sugar-modifications, such as CSF114(GlcNAc), modified with a residue of N-acetylglucosamine, and CSF114[Lys 7 (1-deoxyfructopyranosyl)], this last one modified with a 1-deoxyfructopyranosyl moiety on a lysine at position 7. The analysis was set up using a synthetic compound specifically deuterated on the C-1 to compare its fragmentation with the fragmentation of the undeuterated form, and thus ascertain with confidence the presence on an Asn(Glc) within a peptide sequence. At the end of the study, our analysis led to the identification of signature neutral losses inside the sugar moieties to characterize the different types of glycosylation/glycation. The interest of this study lies in the possibility of applyimg this approach to the discovery of biomarkers and in the diagnosis of autoimmune diseases.

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Section: Sugar-peptide Analogs Of Csf114supporting

confidence: 55%

Multi-Stage Mass Spectrometry Analysis of Sugar-Conjugated β-Turn Structures to be Used as Probes in Autoimmune Diseases

Gentilini

Auberger

Rentier

et al. 2016

J. Am. Soc. Mass Spectrom.

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“…Consequently, low quality spectra are produced because of a poor production of sequence specific ions from the peptide backbone. Signals corresponding to ions generated by losses of specific neutral fragments preferentially dominate the mass spectrum with a reduced success in peptide identification (31,32). This well characterized fragmentation pattern has been recently used by Zhang et al (24) in data-dependent MS3 by neutral loss scanning and pseudo-MS3 by multistage activation.…”

Section: Optimization Of Methods For Analysis Of Glycated Proteinsmentioning

confidence: 99%

Glycation Isotopic Labeling with 13C-Reducing Sugars for Quantitative Analysis of Glycated Proteins in Human Plasma

Priego-Capote

Scherl

Müller

et al. 2010

Molecular & Cellular Proteomics

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Non-enzymatic glycation of proteins is a post-translational modification produced by a reaction between reducing sugars and amino groups located in lysine and arginine residues or in the N-terminal position. This modification plays a relevant role in medicine and food industry. In the clinical field, this undesired role is directly linked to blood glucose concentration and therefore to pathological conditions derived from hyperglycemia (>11 mM glucose) such as diabetes mellitus or renal failure. An approach for qualitative and quantitative analysis of glycated proteins is here proposed to achieve the three information levels for their complete characterization. These are: 1) identification of glycated proteins, 2) elucidation of sugar attachment sites, and 3) quantitative analysis to compare glycemic states. Qualitative analysis was carried out by tandem mass spectrometry after endoproteinase Glu-C digestion and boronate affinity chromatography for isolation of glycated peptides. For this purpose, two MS operational modes were used: higher energy collisional dissociation-MS2

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“…The given series of neutral losses is characteristic for Amadori products and enables the differentiation of these compounds from the products of enzymatic O-or N-glycosylation. [9] Although the fragmentation behavior of the glycated peptides is well studied and widely utilized in analysis, there is limited information on the mechanistic aspects of these fragmentations.…”

Section: Introductionmentioning

confidence: 99%

A mechanistic study on the fragmentation of peptide‐derived Amadori products

et al. 2009

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Gas phase fragmentation of peptide-derived Amadori products was investigated using synthetic compounds regioselectively deuterated as well as labeled with 18O at aminofructose moiety. The eliminated molecule CH2O contains exclusively protons attached to carbon C6 of the aminofructose moiety. The hydrogen atoms connected with the carbon C1 of the aminofructose moiety are partially eliminated as a component of water molecules during the dehydration process and partially dislocated within the fragmented peptide molecule. The labeled oxygen atom attached to the carbon C2 is eliminated in 100% along with the first loss of water. The MS3 experiments revealed that the product ion formed by triple dehydration of the Amadori product does not eliminate the formaldehyde molecule. On the basis of these observations we proposed a hypothetical mechanism of Amadori products' fragmentation.

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Fragmentation behavior of glycated peptides derived from D‐glucose, D‐fructose and D‐ribose in tandem mass spectrometry

Cited by 101 publications

References 32 publications

Multi-Stage Mass Spectrometry Analysis of Sugar-Conjugated β-Turn Structures to be Used as Probes in Autoimmune Diseases

Multi-Stage Mass Spectrometry Analysis of Sugar-Conjugated β-Turn Structures to be Used as Probes in Autoimmune Diseases

Glycation Isotopic Labeling with 13C-Reducing Sugars for Quantitative Analysis of Glycated Proteins in Human Plasma

A mechanistic study on the fragmentation of peptide‐derived Amadori products

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