Study of an unusual advanced glycation end-product (AGE) derived from glyoxal using mass spectrometry

Andrea F. Lopez-Clavijo; Carlos A. Duque-Daza; Isolda Romero Canelon; Mark P. Barrow; David Kilgour; Naila Rabbani; Paul J. Thornalley; Peter B. O'Connor

doi:10.1007/s13361-013-0799-2

Study of an unusual advanced glycation end-product (AGE) derived from glyoxal using mass spectrometry

Andrea F. Lopez-Clavijo, Carlos A. Duque-Daza, Isolda Romero Canelon, Mark P. Barrow, David Kilgour, Naila Rabbani, Paul J. Thornalley, Peter B. O'Connor^*

^*Corresponding author for this work

Pharmacy

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

Abstract

(Chemical Presented) Glycation is a post-translational modification (PTM) that affects the physiological properties of peptides and proteins. In particular, during hyperglycaemia, glycation by α-dicarbonyl compounds generate α-dicarbonyl-derived glycation products also called α-dicarbonyl-derived advanced glycation end products. Glycation by the α-dicarbonyl compound known as glyoxal was studied in model peptides by MS/MS using a Fourier transform ion cyclotron resonance mass spectrometer. An unusual type of glyoxal-derived AGE with a mass addition of 21.98436 Da is reported in peptides containing combinations of two arginine-two lysine, and one arginine-three lysine amino acid residues. Electron capture dissociation and collisionally activated dissociation results supported that the unusual glyoxal-derived AGE is formed at the guanidino group of arginine, and a possible structure is proposed to illustrate the 21.9843 Da mass addition.

Original language	English
Pages (from-to)	673-683
Number of pages	11
Journal	Journal of the American Society for Mass Spectrometry
Volume	25
Issue number	4
Early online date	28 Jan 2014
DOIs	https://doi.org/10.1007/s13361-013-0799-2
Publication status	Published - Apr 2014

Keywords

Advanced glycation endproducts (AGEs)
Collision-induced dissociation (CID)
Collisionally activated dissociation (CAD)
Electron capture dissociation (ECD)
Glycation
Glyoxal
Maillard reaction
Mass spectrometry
PTMs

ASJC Scopus subject areas

Structural Biology
Spectroscopy

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title = "Study of an unusual advanced glycation end-product (AGE) derived from glyoxal using mass spectrometry",

abstract = "(Chemical Presented) Glycation is a post-translational modification (PTM) that affects the physiological properties of peptides and proteins. In particular, during hyperglycaemia, glycation by α-dicarbonyl compounds generate α-dicarbonyl-derived glycation products also called α-dicarbonyl-derived advanced glycation end products. Glycation by the α-dicarbonyl compound known as glyoxal was studied in model peptides by MS/MS using a Fourier transform ion cyclotron resonance mass spectrometer. An unusual type of glyoxal-derived AGE with a mass addition of 21.98436 Da is reported in peptides containing combinations of two arginine-two lysine, and one arginine-three lysine amino acid residues. Electron capture dissociation and collisionally activated dissociation results supported that the unusual glyoxal-derived AGE is formed at the guanidino group of arginine, and a possible structure is proposed to illustrate the 21.9843 Da mass addition.",

keywords = "Advanced glycation endproducts (AGEs), Collision-induced dissociation (CID), Collisionally activated dissociation (CAD), Electron capture dissociation (ECD), Glycation, Glyoxal, Maillard reaction, Mass spectrometry, PTMs",

author = "Lopez-Clavijo, {Andrea F.} and Duque-Daza, {Carlos A.} and {Romero Canelon}, Isolda and Barrow, {Mark P.} and David Kilgour and Naila Rabbani and Thornalley, {Paul J.} and O'Connor, {Peter B.}",

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AU - Lopez-Clavijo, Andrea F.

AU - Duque-Daza, Carlos A.

AU - Romero Canelon, Isolda

AU - Barrow, Mark P.

AU - Kilgour, David

AU - Rabbani, Naila

AU - Thornalley, Paul J.

AU - O'Connor, Peter B.

PY - 2014/4

Y1 - 2014/4

N2 - (Chemical Presented) Glycation is a post-translational modification (PTM) that affects the physiological properties of peptides and proteins. In particular, during hyperglycaemia, glycation by α-dicarbonyl compounds generate α-dicarbonyl-derived glycation products also called α-dicarbonyl-derived advanced glycation end products. Glycation by the α-dicarbonyl compound known as glyoxal was studied in model peptides by MS/MS using a Fourier transform ion cyclotron resonance mass spectrometer. An unusual type of glyoxal-derived AGE with a mass addition of 21.98436 Da is reported in peptides containing combinations of two arginine-two lysine, and one arginine-three lysine amino acid residues. Electron capture dissociation and collisionally activated dissociation results supported that the unusual glyoxal-derived AGE is formed at the guanidino group of arginine, and a possible structure is proposed to illustrate the 21.9843 Da mass addition.

AB - (Chemical Presented) Glycation is a post-translational modification (PTM) that affects the physiological properties of peptides and proteins. In particular, during hyperglycaemia, glycation by α-dicarbonyl compounds generate α-dicarbonyl-derived glycation products also called α-dicarbonyl-derived advanced glycation end products. Glycation by the α-dicarbonyl compound known as glyoxal was studied in model peptides by MS/MS using a Fourier transform ion cyclotron resonance mass spectrometer. An unusual type of glyoxal-derived AGE with a mass addition of 21.98436 Da is reported in peptides containing combinations of two arginine-two lysine, and one arginine-three lysine amino acid residues. Electron capture dissociation and collisionally activated dissociation results supported that the unusual glyoxal-derived AGE is formed at the guanidino group of arginine, and a possible structure is proposed to illustrate the 21.9843 Da mass addition.

KW - Advanced glycation endproducts (AGEs)

KW - Collision-induced dissociation (CID)

KW - Collisionally activated dissociation (CAD)

KW - Electron capture dissociation (ECD)

KW - Glycation

KW - Glyoxal

KW - Maillard reaction

KW - Mass spectrometry

KW - PTMs

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AN - SCOPUS:84896985684

SN - 1044-0305

VL - 25

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EP - 683

JO - Journal of the American Society for Mass Spectrometry

JF - Journal of the American Society for Mass Spectrometry

IS - 4

ER -

Study of an unusual advanced glycation end-product (AGE) derived from glyoxal using mass spectrometry

Abstract

Keywords

ASJC Scopus subject areas

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