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. 2007;21(5):661-6.
doi: 10.1002/rcm.2884.

Application of electron transfer dissociation mass spectrometry in analyses of non-enzymatically glycated peptides

Qibin Zhang  1 , Andrej Frolov, Ning Tang, Ralf Hoffmann, Tom van de Goor, Thomas O Metz, Richard D Smith
Affiliations

Application of electron transfer dissociation mass spectrometry in analyses of non-enzymatically glycated peptides

Qibin Zhang et al. Rapid Commun Mass Spectrom. 2007.

Abstract

Non-enzymatic glycation of peptides and proteins by D-glucose has important implications in the pathogenesis of diabetes mellitus, particularly in the context of development of diabetic complications. The fragmentation behavior of glycated peptides produced from reaction of D-glucose with lysine residues was investigated by electron transfer dissociation (ETD) and collision-induced dissociation (CID) tandem mass spectrometry. It was found that high abundance ions corresponding to various degrees of neutral water losses, as well as furylium ion production, dominate the CID spectra, and that the sequence-informative b and y ions were rarely observed when Amadori-modified peptides were fragmented. Contrary to what was observed under CID conditions, ions corresponding to neutral losses of water or furylium ion production were not observed in the ETD spectra. Instead, abundant and almost complete series of c- and z-type ions were observed regardless of whether the modification site was located in the middle of the sequence or close to the N-terminus, greatly facilitating the peptide sequencing. This study strongly suggests that ETD is a better technique for proteomic studies of non-enzymatically glycated peptides and proteins.

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Figures

Figure 1
Figure 1
Structure of the Amadori compound (AC) resulting from reaction of primary amino groups with glucose, and structure of the furylium ion, which is formed during the collision induced dissociation process by loss of 3 H2O and HCHO.
Figure 2
Figure 2
ETD (a) and CID (b) MS/MS spectra of the [M+2H]2+ ion of peptide AGGK#AAFL-NH2, in which # represents glucose adduct to lysine. The spectra were acquired with alternating ETD and CID scanning.
Figure 3
Figure 3
ETD (a) and CID (b) MS/MS spectra of the [M+2H]2+ ion of peptide AK#ASASFL-NH2, in which # represents glucose adduct to lysine. The spectra were acquired with alternating ETD and CID scanning.
Figure 4
Figure 4
ETD (a) and CID (b) MS/MS spectra of the [M+2H]2+ of peptide AK#DSASFL-NH2, in which # represents glucose adduct to lysine. The spectra were acquired with alternating ETD and CID scanning.
Figure 5
Figure 5
MS3 spectrum of the [M+H]+ ion of peptide AGGK#AAFL-NH2 under CID conditions, in which # represents glucose adduct to lysine. Shown is the MS/MS of [M+H-84]+ generated in the first stage MS/MS of the [M+H]+ ion.
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References

    1. Baynes JW, Watkins NG, Fisher CI, Hull CJ, Patrick JS, Ahmed MU, Dunn JA, Thorpe SR. Prog. Clin. Biol. Res. 1989;304:43. - PubMed
    1. Ahmed N, Thornalley PJ. Biochem. Soc. Trans. 2003;31:1417. - PubMed
    1. Krishnamurti U, Steffes MW. Clin. Chem. 2001;47:1157. - PubMed
    1. Thorpe SR, Baynes JW. Drugs & Aging. 1996;9:69. - PubMed
    1. Mosier MA, Occhipinti JR, Burstein NL. Arch. Opthalmol. 1986;104:1340. - PubMed

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