Production of lysozyme and lysozyme-superoxide dismutase dimers bound by a ditryptophan cross-link in carbonate radical-treated lysozyme

Paviani, Verônica; Queiroz, Raphael Ferreira; Marques, Emerson Finco; Mascio, Paolo Di; Augusto, Ohára

doi:10.1016/j.freeradbiomed.2015.07.015

Cited by 45 publications

(62 citation statements)

References 62 publications

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“…21 The spent reaction was analyzed by LC-MS/MS and we were surprised to observe three peaks with m/z values of 407.17, which correspond to Trp-Trp and were not present in the control (Figure 4). These results indicated that three Trp-Trp isomers were produced on treatment of Trp (1 mM) with photolitically generated CO 3…”

Section: On the Structure Of Trp-trp Cross-links Produced By Radical mentioning

confidence: 96%

“…21 This resulted in oxidation of lysozyme at Trp28 (lysozymeTrp28 • ), which dimerized to form lysozymeTrp28-Trp28lysozyme, and inactivation and aggregation of the enzyme. The lysozymeTrp28-Trp28lysozyme dimer also formed when the enzyme was treated with UVC light for longer times than those used to generate the CO 3…”

Section: Trp-trp Cross-links As Novel Products Of Protein Oxidationmentioning

confidence: 99%

“…21,58 While testing CO 3 •− in the development of synthetic procedures, we treated Trp (1 mM) with CO 3…”

Section: On the Structure Of Trp-trp Cross-links Produced By Radical mentioning

confidence: 99%

“…19 Subsequent to this publication, a number of reports described the formation of Trp-Trp cross-links during peptide and protein oxidation, by a variety of oxidizing systems. [20][21][22][23][24][25] Thus, the time has come to summarize these studies, emphasizing the challenges to characterize Trp-Trp cross-links and their potential roles in protein dysfunction and aggregation.…”

Section: Protein Oxidationmentioning

confidence: 99%

“…20 In another example, we treated the enzyme lysozyme with enzymatically-or photolytically-generated CO 3 •− . 21 This resulted in oxidation of lysozyme at Trp28 (lysozymeTrp28 • ), which dimerized to form lysozymeTrp28-Trp28lysozyme, and inactivation and aggregation of the enzyme. The lysozymeTrp28-Trp28lysozyme dimer also formed when the enzyme was treated with UVC light for longer times than those used to generate the CO 3 •− from carbonatotetramminecobalt(III) complex photolysis (1 min) (Figure 3).…”

Section: Trp-trp Cross-links As Novel Products Of Protein Oxidationmentioning

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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Section: On the Structure Of Trp-trp Cross-links Produced By Radical mentioning

confidence: 96%

Section: Trp-trp Cross-links As Novel Products Of Protein Oxidationmentioning

confidence: 99%

“…21,58 While testing CO 3 •− in the development of synthetic procedures, we treated Trp (1 mM) with CO 3…”

Section: On the Structure Of Trp-trp Cross-links Produced By Radical mentioning

confidence: 99%

Section: Protein Oxidationmentioning

confidence: 99%

Section: Trp-trp Cross-links As Novel Products Of Protein Oxidationmentioning

confidence: 99%

See 3 more Smart Citations

Ditryptophan Cross-Links as Novel Products of Protein Oxidation

Paviani

Galdino

Prazeres

et al. 2017

J. Braz. Chem. Soc.

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Chemical repair of damaged leucine and tryptophane by thiophenols at close to diffusion‐controlled rates: Mechanisms and kinetics

et al. 2022

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Thiophenols are chemical species with multiple desirable biological properties, including their primary and secondary antioxidant capacity. In this work, the repairing antioxidant activity of eight different thiophenols has been investigated for damaged leucine and tryptophane. The investigation was carried out employing quantum mechanical and transition state methods to calculate the thermodynamic and kinetic data of the reactions involved, while simulating the biological conditions at physiological pH and aqueous and lipidic medium. The analysis of the atomic charges and the spin densities at each of the points on the potential energy surface was the tool that allowed the elucidation of the reaction mechanisms through which thiophenols repair the oxidative damage caused to the amino acids leucine and tryptophan. It was found that thiophenols can repair leucine via a hydrogen atom transfer mechanism in a manner which is similar to the one used by glutathione to repair the carbon-centered radicals of guanosine. In addition, thiophenols can also restore tryptophane, a nitrogen-centered radical, via proton-coupled electron transfer and single electron transfer mechanisms. Moreover, both processes occur at close to diffusion-controlled rates.

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Singlet oxygen‐induced protein aggregation: Lysozyme crosslink formation and nLC‐MS/MS characterization

2019

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Singlet molecular oxygen ( 1 O 2 ) has been associated with a number of physiological processes. Despite the recognized importance of 1 O 2 -mediated protein modifications, little is known about the role of this oxidant in crosslink formation and protein aggregation. Thus, using lysozyme as a model, the present study sought to investigate the involvement of 1 O 2 in crosslink formation. Lysozyme was photochemically oxidized in the presence of rose bengal or chemically oxidized using [ 18 O]-labeled 1 O 2 released from thermolabile endoperoxides. It was concluded that both 1 O 2 generating systems induce lysozyme crosslinking and aggregation. Using SDS-PAGE and nanoscale liquid chromatography coupled to electrospray ionization mass spectrometry, the results clearly demonstrated that 1 O 2 is directly involved in the formation of covalent crosslinks involving the amino acids histidine, lysine, and tryptophan.

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Production of lysozyme and lysozyme-superoxide dismutase dimers bound by a ditryptophan cross-link in carbonate radical-treated lysozyme

Cited by 45 publications

References 62 publications

Ditryptophan Cross-Links as Novel Products of Protein Oxidation

Ditryptophan Cross-Links as Novel Products of Protein Oxidation

Chemical repair of damaged leucine and tryptophane by thiophenols at close to diffusion‐controlled rates: Mechanisms and kinetics

Singlet oxygen‐induced protein aggregation: Lysozyme crosslink formation and nLC‐MS/MS characterization

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