Quantification of hydroxyl radical-derived oxidation products in peptides containing glycine, alanine, valine, and proline
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Quantification of hydroxyl radical-derived oxidation products in peptides containing glycine, alanine, valine, and proline. / Morgan, Philip E; Pattison, David I; Davies, Michael Jonathan.
In: Free Radical Biology & Medicine, Vol. 52, No. 2, 15.01.2012, p. 328-39.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Quantification of hydroxyl radical-derived oxidation products in peptides containing glycine, alanine, valine, and proline
AU - Morgan, Philip E
AU - Pattison, David I
AU - Davies, Michael Jonathan
N1 - Copyright © 2011 Elsevier Inc. All rights reserved.
PY - 2012/1/15
Y1 - 2012/1/15
N2 - Proteins are a major target for oxidation due to their abundance and high reactivity. Despite extensive investigation over many years, only limited quantitative data exist on the contributions of different pathways to the oxidation of peptides and proteins. This study was designed to obtain quantitative data on the nature and yields of oxidation products (alcohols, carbonyls, hydroperoxides, fragment species) formed by a prototypic oxidant system (HO(•)/O(2)) on small peptides of limited, but known, amino acid composition. Peptides composed of Gly, Ala, Val, and Pro were examined with particular emphasis on the peptide Val-Gly-Val-Ala-Pro-Gly, a repeat motif in elastin with chemotactic activity and metalloproteinase regulation properties. The data obtained indicate that hydroperoxide formation occurs nonrandomly (Pro > Val > Ala > Gly) with this inversely related to carbonyl yields (both peptide-bound and released). Multiple alcohols are generated at both side-chain and backbone sites. Backbone fragmentation has been characterized at multiple positions, with sites adjacent to Pro residues being of major importance. Summation of the product concentrations provides clear evidence for the occurrence of chain reactions in peptides exposed to HO(•)/O(2), with the overall product yields exceeding that of the initial HO(•) generated.
AB - Proteins are a major target for oxidation due to their abundance and high reactivity. Despite extensive investigation over many years, only limited quantitative data exist on the contributions of different pathways to the oxidation of peptides and proteins. This study was designed to obtain quantitative data on the nature and yields of oxidation products (alcohols, carbonyls, hydroperoxides, fragment species) formed by a prototypic oxidant system (HO(•)/O(2)) on small peptides of limited, but known, amino acid composition. Peptides composed of Gly, Ala, Val, and Pro were examined with particular emphasis on the peptide Val-Gly-Val-Ala-Pro-Gly, a repeat motif in elastin with chemotactic activity and metalloproteinase regulation properties. The data obtained indicate that hydroperoxide formation occurs nonrandomly (Pro > Val > Ala > Gly) with this inversely related to carbonyl yields (both peptide-bound and released). Multiple alcohols are generated at both side-chain and backbone sites. Backbone fragmentation has been characterized at multiple positions, with sites adjacent to Pro residues being of major importance. Summation of the product concentrations provides clear evidence for the occurrence of chain reactions in peptides exposed to HO(•)/O(2), with the overall product yields exceeding that of the initial HO(•) generated.
KW - Alanine
KW - Alcohols
KW - Amino Acid Sequence
KW - Gamma Rays
KW - Glycine
KW - Hydrogen Peroxide
KW - Hydroxyl Radical
KW - Molecular Weight
KW - Oxidation-Reduction
KW - Oxygen
KW - Peptides
KW - Proline
KW - Protein Carbonylation
KW - Proteolysis
KW - Tandem Mass Spectrometry
KW - Valine
U2 - 10.1016/j.freeradbiomed.2011.10.448
DO - 10.1016/j.freeradbiomed.2011.10.448
M3 - Journal article
C2 - 22064365
VL - 52
SP - 328
EP - 339
JO - Free Radical Biology & Medicine
JF - Free Radical Biology & Medicine
SN - 0891-5849
IS - 2
ER -
ID: 128975229