Light-Induced Conversion of Trp to Gly and Gly Hydroperoxide in IgG1

Haywood, Jessica; Mozziconacci, Olivier; Allegre, Kevin M.; Kerwin, Bruce A.; Schöneich, Christian

doi:10.1021/mp300680c

Cited by 42 publications

(44 citation statements)

References 25 publications

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“…Current literature32, 33, 34 describes only photolytic C α −C β bond cleavage. However, this PTM is also observed in the non‐irradiated bone controls, indicating that this modification might also be due to aging rather than exclusively being UV‐mediated.…”

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confidence: 99%

Palaeoproteomic Profiling of Conservation Layers on a 14th Century Italian Wall Painting

et al. 2018

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Ahead of display, a non‐original layer was observed on the surface of a fragment of a wall painting by Ambrogio Lorenzetti (active 1319, died 1348/9). FTIR analysis suggested proteinaceous content. Mass spectrometry was used to better characterise this layer and revealed two protein components: sheep and cow glue and chicken and duck egg white. Analysis of post‐translational modifications detected several photo‐oxidation products, which suggest that the egg experienced prolonged exposure to UV light and was likely applied long before the glue layer. Additionally, glycation products detected may indicate naturally occurring glycoprotein degradation or reaction with a carbohydrate material such as starch, identified by ATR‐FTIR in a cross‐section of a sample taken from the painting. Palaeoproteomics is shown to provide detailed characterisation of organic layers associated with mural paintings and therefore aids reconstruction of the conservation history of these objects.

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confidence: 99%

Palaeoproteomic Profiling of Conservation Layers on a 14th Century Italian Wall Painting

et al. 2018

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Section: Oxidation Of Protein-trp Residuesmentioning

confidence: 99%

“…These pharmaceuticals can degrade via multiple physical and chemical processes, including protein photo-oxidation and aggregation. 13,14 A better knowledge of these processes is necessary to prevent degradation and to maintain the stability of protein pharmaceuticals.…”

Section: Protein Oxidationmentioning

confidence: 99%

“…14,19,[26][27][28][29][30] On the other hand, Trp residues are the strongest UV chromophore in proteins, rendering diverse products through a rich photochemistry involving both protein-Trp • and 1 O 2 -mediated pathways ( Figure 1). 31,32 Despite the low frequency of Trp residues in proteins, they have a unique potential to interact with other proteins and cellular structures.…”

Section: Oxidation Of Protein-trp Residuesmentioning

confidence: 99%

“…926 and aggregation. 13,14 A better knowledge of these processes is necessary to prevent degradation and to maintain the stability of protein pharmaceuticals.Despite the potential of protein-protein cross-links constituting protein aggregation-prone intermediates, the chemical nature of these bonds remains only partially characterized. Among the reasons for this situation is the lack of bioinformatic tools to analyze LC-MS/MS (liquid chromatography tandem mass spectrometry) proteomic data related to protein-protein cross-links, 15 although these tools are currently under development.…”

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confidence: 99%

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Ditryptophan Cross-Links as Novel Products of Protein Oxidation

Paviani

Galdino

Prazeres

et al. 2017

J. Braz. Chem. Soc.

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Protein oxidation is an unavoidable consequence of aerobic metabolism. The oxidation of most proteins residues is non-repairable and may affect protein structure and function. In particular, protein cross-links arising from oxidative modifications are presumably toxic to cells because they may accumulate and induce protein aggregation. However, most of these irreversible protein cross-links remain partially characterized. Up to very recently, ditryptophan cross-links (Trp-Trp), in particular, have been largely disregarded in the literature. Here, we briefly review studies showing that Trp-Trp cross-links can be formed in proteins exposed to a variety of oxidants. The challenges to fully characterize Trp-Trp cross-links are discussed as well as their potential roles in protein dysfunction and aggregation.Keywords: ditryptophan, cross-links, protein oxidation, free radicals Protein OxidationFree radicals and other oxidants are formed in living organisms by oxidation-reduction processes, which occur continuously during metabolism and through interactions with the environment. Organisms evolved enzymatic antioxidant defenses and the capability to use antioxidants from the diet to control the levels of these species. 1,2 Nevertheless, under certain circumstances, the levels of radicals and oxidants increase, promoting the oxidation of biomolecules. Among them, proteins are the major targets, due to their high biological abundance and reactivity towards one-and two-electron oxidants. [3][4][5] Protein residues most susceptible to oxidation are the sulfur-containing residues Cys and Met, and the aromatic residues His, Phe, Tyr, and Trp. In vivo, the oxidation of Cys and Met residues can be reversed by biological reductants with the assistance of enzymatic systems. In fact, the reversible oxidation of protein-Cys residues is emerging as a fundamental cell regulatory mechanism. 2,[6][7][8] The oxidation of all the other protein residues is irreversible, and includes several covalent modifications, such as protein cleavage, carbonylation, nitration, hydroxylation, halogenation and protein cross-linking with other proteins, lipids, carbohydrates and nucleic acids. [3][4][5][9][10][11] These modifications result in protein fragmentation, loss of protein function, protein aggregation and/or altered protein turnover, leading to cell and tissue dysfunction and various human pathologies. To maintain cellular homeostasis, proteins irreversibly oxidized are targeted for degradation by the proteasomal and lysosomal degradation pathways.11,12 During aging and pathological conditions associated with oxidative stress, however, the levels of over-oxidized and cross-linked proteins accumulate because these species are poor substrates for the intracellular proteolytic systems. This may lead to protein aggregation, which is a hallmark of age-related diseases, such as neurodegenerative diseases, atherosclerosis and cataract.11,12 Therefore, the study of irreversible protein oxidation in vitro and in vivo is relevant to the understanding o...

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Palaeoproteomic Profiling of Conservation Layers on a 14th Century Italian Wall Painting

et al. 2018

View full text Add to dashboard Cite

Ahead of display, anon-original layer was observed on the surface of af ragment of aw all painting by Ambrogio Lorenzetti (active 1319, died 1348/9). FTIR analysis suggested proteinaceous content. Mass spectrometry was used to better characterise this layer and revealed two protein components: sheep and cow glue and chicken and duckegg white.Analysis of post-translational modifications detected several photooxidation products,w hichs uggest that the egg experienced prolonged exposure to UV light and was likely applied long before the glue layer.Additionally,glycation products detected may indicate naturally occurring glycoprotein degradation or reaction with acarbohydrate material such as starch,identified by ATR-FTIR in ac ross-section of as ample taken from the painting.P alaeoproteomics is shown to provide detailed characterisation of organic layers associated with mural paintings and therefore aids reconstruction of the conservation history of these objects.

show abstract

Light-Induced Conversion of Trp to Gly and Gly Hydroperoxide in IgG1

Cited by 42 publications

References 25 publications

Palaeoproteomic Profiling of Conservation Layers on a 14th Century Italian Wall Painting

Palaeoproteomic Profiling of Conservation Layers on a 14th Century Italian Wall Painting

Ditryptophan Cross-Links as Novel Products of Protein Oxidation

Palaeoproteomic Profiling of Conservation Layers on a 14th Century Italian Wall Painting

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