Chemical modification of lysozyme, glucose 6-phosphate dehydrogenase, and bovine eye lens proteins induced by peroxyl radicals: role of oxidizable amino acid residues

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Chemical modification of lysozyme, glucose 6-phosphate dehydrogenase, and bovine eye lens proteins induced by peroxyl radicals : role of oxidizable amino acid residues. / Arenas, Andrea; López-Alarcón, Camilo; Kogan, Marcelo; Lissi, Eduardo; Davies, Michael Jonathan; Silva, Eduardo.

In: Chemical Research in Toxicology, Vol. 26, No. 1, 18.01.2013, p. 67-77.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Arenas, A, López-Alarcón, C, Kogan, M, Lissi, E, Davies, MJ & Silva, E 2013, 'Chemical modification of lysozyme, glucose 6-phosphate dehydrogenase, and bovine eye lens proteins induced by peroxyl radicals: role of oxidizable amino acid residues', Chemical Research in Toxicology, vol. 26, no. 1, pp. 67-77. https://doi.org/10.1021/tx300372t

APA

Arenas, A., López-Alarcón, C., Kogan, M., Lissi, E., Davies, M. J., & Silva, E. (2013). Chemical modification of lysozyme, glucose 6-phosphate dehydrogenase, and bovine eye lens proteins induced by peroxyl radicals: role of oxidizable amino acid residues. Chemical Research in Toxicology, 26(1), 67-77. https://doi.org/10.1021/tx300372t

Vancouver

Arenas A, López-Alarcón C, Kogan M, Lissi E, Davies MJ, Silva E. Chemical modification of lysozyme, glucose 6-phosphate dehydrogenase, and bovine eye lens proteins induced by peroxyl radicals: role of oxidizable amino acid residues. Chemical Research in Toxicology. 2013 Jan 18;26(1):67-77. https://doi.org/10.1021/tx300372t

Author

Arenas, Andrea ; López-Alarcón, Camilo ; Kogan, Marcelo ; Lissi, Eduardo ; Davies, Michael Jonathan ; Silva, Eduardo. / Chemical modification of lysozyme, glucose 6-phosphate dehydrogenase, and bovine eye lens proteins induced by peroxyl radicals : role of oxidizable amino acid residues. In: Chemical Research in Toxicology. 2013 ; Vol. 26, No. 1. pp. 67-77.

Bibtex

@article{5473e9beea2849659dfbe83f37c5ac2b,
title = "Chemical modification of lysozyme, glucose 6-phosphate dehydrogenase, and bovine eye lens proteins induced by peroxyl radicals: role of oxidizable amino acid residues",
abstract = "Chemical and structural alterations to lysozyme (LYSO), glucose 6-phosphate dehydrogenase (G6PD), and bovine eye lens proteins (BLP) promoted by peroxyl radicals generated by the thermal decomposition of 2,2'-azobis(2-amidinopropane) hydrochloride (AAPH) under aerobic conditions were investigated. SDS-PAGE analysis of the AAPH-treated proteins revealed the occurrence of protein aggregation, cross-linking, and fragmentation; BLP, which are naturally organized in globular assemblies, were the most affected proteins. Transmission electron microscopy (TEM) analysis of BLP shows the formation of complex protein aggregates after treatment with AAPH. These structural modifications were accompanied by the formation of protein carbonyl groups and protein hydroperoxides. The yield of carbonyls was lower than that for protein hydroperoxide generation and was unrelated to protein fragmentation. The oxidized proteins were also characterized by significant oxidation of Met, Trp, and Tyr (but not other) residues, and low levels of dityrosine. As the dityrosine yield is too low to account for the observed cross-linking, we propose that aggregation is associated with tryptophan oxidation and Trp-derived cross-links. It is also proposed that Trp oxidation products play a fundamental role in nonrandom fragmentation and carbonyl group formation particularly for LYSO and G6PD. These data point to a complex mechanism of peroxyl-radical mediated modification of proteins with monomeric (LYSO), dimeric (G6PD), and multimeric (BLP) structural organization, which not only results in oxidation of protein side chains but also gives rise to radical-mediated protein cross-links and fragmentation, with Trp species being critical intermediates.",
keywords = "Amidines, Amino Acids, Animals, Cattle, Crystallins, Dimerization, Electrophoresis, Polyacrylamide Gel, Glucosephosphate Dehydrogenase, Hydrogen Peroxide, Muramidase, Oxidation-Reduction, Peroxides, Protein Carbonylation, Spectrophotometry, Tyrosine",
author = "Andrea Arenas and Camilo L{\'o}pez-Alarc{\'o}n and Marcelo Kogan and Eduardo Lissi and Davies, {Michael Jonathan} and Eduardo Silva",
year = "2013",
month = "1",
day = "18",
doi = "10.1021/tx300372t",
language = "English",
volume = "26",
pages = "67--77",
journal = "Chemical Research in Toxicology",
issn = "0893-228X",
publisher = "American Chemical Society",
number = "1",

}

RIS

TY - JOUR

T1 - Chemical modification of lysozyme, glucose 6-phosphate dehydrogenase, and bovine eye lens proteins induced by peroxyl radicals

T2 - role of oxidizable amino acid residues

AU - Arenas, Andrea

AU - López-Alarcón, Camilo

AU - Kogan, Marcelo

AU - Lissi, Eduardo

AU - Davies, Michael Jonathan

AU - Silva, Eduardo

PY - 2013/1/18

Y1 - 2013/1/18

N2 - Chemical and structural alterations to lysozyme (LYSO), glucose 6-phosphate dehydrogenase (G6PD), and bovine eye lens proteins (BLP) promoted by peroxyl radicals generated by the thermal decomposition of 2,2'-azobis(2-amidinopropane) hydrochloride (AAPH) under aerobic conditions were investigated. SDS-PAGE analysis of the AAPH-treated proteins revealed the occurrence of protein aggregation, cross-linking, and fragmentation; BLP, which are naturally organized in globular assemblies, were the most affected proteins. Transmission electron microscopy (TEM) analysis of BLP shows the formation of complex protein aggregates after treatment with AAPH. These structural modifications were accompanied by the formation of protein carbonyl groups and protein hydroperoxides. The yield of carbonyls was lower than that for protein hydroperoxide generation and was unrelated to protein fragmentation. The oxidized proteins were also characterized by significant oxidation of Met, Trp, and Tyr (but not other) residues, and low levels of dityrosine. As the dityrosine yield is too low to account for the observed cross-linking, we propose that aggregation is associated with tryptophan oxidation and Trp-derived cross-links. It is also proposed that Trp oxidation products play a fundamental role in nonrandom fragmentation and carbonyl group formation particularly for LYSO and G6PD. These data point to a complex mechanism of peroxyl-radical mediated modification of proteins with monomeric (LYSO), dimeric (G6PD), and multimeric (BLP) structural organization, which not only results in oxidation of protein side chains but also gives rise to radical-mediated protein cross-links and fragmentation, with Trp species being critical intermediates.

AB - Chemical and structural alterations to lysozyme (LYSO), glucose 6-phosphate dehydrogenase (G6PD), and bovine eye lens proteins (BLP) promoted by peroxyl radicals generated by the thermal decomposition of 2,2'-azobis(2-amidinopropane) hydrochloride (AAPH) under aerobic conditions were investigated. SDS-PAGE analysis of the AAPH-treated proteins revealed the occurrence of protein aggregation, cross-linking, and fragmentation; BLP, which are naturally organized in globular assemblies, were the most affected proteins. Transmission electron microscopy (TEM) analysis of BLP shows the formation of complex protein aggregates after treatment with AAPH. These structural modifications were accompanied by the formation of protein carbonyl groups and protein hydroperoxides. The yield of carbonyls was lower than that for protein hydroperoxide generation and was unrelated to protein fragmentation. The oxidized proteins were also characterized by significant oxidation of Met, Trp, and Tyr (but not other) residues, and low levels of dityrosine. As the dityrosine yield is too low to account for the observed cross-linking, we propose that aggregation is associated with tryptophan oxidation and Trp-derived cross-links. It is also proposed that Trp oxidation products play a fundamental role in nonrandom fragmentation and carbonyl group formation particularly for LYSO and G6PD. These data point to a complex mechanism of peroxyl-radical mediated modification of proteins with monomeric (LYSO), dimeric (G6PD), and multimeric (BLP) structural organization, which not only results in oxidation of protein side chains but also gives rise to radical-mediated protein cross-links and fragmentation, with Trp species being critical intermediates.

KW - Amidines

KW - Amino Acids

KW - Animals

KW - Cattle

KW - Crystallins

KW - Dimerization

KW - Electrophoresis, Polyacrylamide Gel

KW - Glucosephosphate Dehydrogenase

KW - Hydrogen Peroxide

KW - Muramidase

KW - Oxidation-Reduction

KW - Peroxides

KW - Protein Carbonylation

KW - Spectrophotometry

KW - Tyrosine

U2 - 10.1021/tx300372t

DO - 10.1021/tx300372t

M3 - Journal article

C2 - 23252580

VL - 26

SP - 67

EP - 77

JO - Chemical Research in Toxicology

JF - Chemical Research in Toxicology

SN - 0893-228X

IS - 1

ER -

ID: 128974507