A mechanistic approach towards the formation of bityrosine in proteins by ionizing radiation – GYG model peptide

Sowinski, S.; Varca, Gustavo H.C.; Kadłubowski, Sławomir; Lugão, Ademar B.; Ulański, Piotr

doi:10.1016/j.radphyschem.2021.109644

Cited by 5 publications

(6 citation statements)

References 36 publications

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“…The additional peak of Tyr C ε ′ was also observed at 118.42 ppm, which was attributed to the chemical shift of Tyr C ε owing to cross-linking via bityrosine formation between SF and SF. The result agrees with those in the literature that the aromatic amino acid of Tyr is an important factor for cross-linking protein by forming a Try–Try linkage during irradiation. ,− …”

Section: Results and Discussionsupporting

confidence: 92%

“…As also reported, intermolecular dityrosine (Tyr–Tyr) formation has been implicated in the cross-linking of proteins during irradiation . In recent years, it has been proven that the hydroxyl free radical showed a higher rate of reaction with tyrosine amino acid than the other amino acids in the protein after irradiation using an advanced pulse radiolysis method …”

Section: Results and Discussionmentioning

confidence: 82%

“…69 In recent years, it has been proven that the hydroxyl free radical showed a higher rate of reaction with tyrosine amino acid than the other amino acids in the protein after irradiation using an advanced pulse radiolysis method. 70 Optimizing the SF-PEO Ratio to Meet the Desirable Morphology of Nanofibers. Using different SF/PEO concentration ratios as described, the SF-PEO nanofibers could be fabricated.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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Strengthened Silk-Fibroin/Poly(ethylene oxide) Nonwoven Nanofibers: A Dual Green Process Using Pure Water for Electrospinning and Electron Beam-Assisted Cross-Linking

Wongkrongsak

Pangon

Pongsak

et al. 2022

ACS Sustainable Chem. Eng.

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A combination process of using pure water for electrospinning and electron beam (EB)-assisted cross-linking is proposed as a dual green route to obtain strengthened silk fibroin (SF)-based nonwoven nanofibers toward value-added healthcare or biomedical products. The first challenge is to optimize the electrospinning process using SF/poly(ethylene oxide) (PEO) in a pure water solution for the fabrication of nonwoven nanofibers. Another technological challenge is to stabilize the dissoluble SF/ PEO nonwoven nanofibers through a cross-linking network created by a free radical reaction using EB irradiation. Herein, we optimized SF/PEO combination and the electrospinning parameters for the fabrication of SF-PEO nanofibers. Under mild conditions using an aqueous solution of SF-PEO and tunable electrospinning parameters, elongated, cylindrical-shaped, and smooth SF-PEO nanofibers with a diameter of 169 ± 5 nm were obtained. The stability of the SF-PEO nanofibers could be tuned by EB irradiation with the absorbed doses in the range of 10−100 kGy. Aiming at well-defined characteristics of nanofibers, the morphology, gel fraction, kinetics of swelling behavior, chemical and packing structure, thermal and mechanical properties, cell cytotoxicity, and proliferation were characterized and relatively clarified with the influencing parameters. It is important to note that EB irradiation with a reliable sterilization dose of 25 kGy was an optimum dose for cross-linking. Upon cross-linking the SF-PEO nanofibers, the dissolution of the nanofibers reduced, they became more stable, and their mechanical properties significantly improved with an increase in ductility by ∼22-fold. The cross-linked SF-PEO nanofibers promoted cell proliferation and proved nontoxic to skin fibroblast cells (L929), and they are thus appropriate for healthcare and biomedical applications. This study shows the potential of using 3G approaches, i.e., green renewable polymers, green electrospinning, and a green EB irradiation process, for sustainable chemistry for biomedical engineering applications.

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Section: Results and Discussionsupporting

confidence: 92%

Section: Results and Discussionmentioning

confidence: 82%

Section: ■ Results and Discussionmentioning

confidence: 99%

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Strengthened Silk-Fibroin/Poly(ethylene oxide) Nonwoven Nanofibers: A Dual Green Process Using Pure Water for Electrospinning and Electron Beam-Assisted Cross-Linking

Wongkrongsak

Pangon

Pongsak

et al. 2022

ACS Sustainable Chem. Eng.

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“…Recently, a technological platform based on radiation cross-linked proteins and enzymes has been developed to obtain materials of biomedical importance. In our upcoming publications, we intend to address to important mechanistic aspects of synthesis by irradiation protein and enzymatic aggregates in line with the latest technological findings [ 6 , 60 , 71 , 72 , 73 , 74 ].…”

Section: Discussionmentioning

confidence: 99%

Spontaneous and Ionizing Radiation-Induced Aggregation of Human Serum Albumin: Dityrosine as a Fluorescent Probe

Radomska

Wolszczak

2022

IJMS

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The use of spectroscopic techniques has shown that human serum albumin (HSA) undergoes reversible self-aggregation through protein–protein interactions. It ensures the subsequent overlapping of electron clouds along with the stiffening of the conformation of the interpenetrating network of amino acids of adjacent HSA molecules. The HSA oxidation process related to the transfer of one electron was investigated by pulse radiolysis and photochemical methods. It has been shown that the irradiation of HSA solutions under oxidative stress conditions results in the formation of stable protein aggregates. The HSA aggregates induced by ionizing radiation are characterized by specific fluorescence compared to the emission of non-irradiated solutions. We assume that HSA dimers are mainly responsible for the new emission. Dityrosine produced by the intermolecular recombination of protein tyrosine radicals as a result of radiolysis of an aqueous solution of the protein is the main cause of HSA aggregation by cross-linking. Analysis of the oxidation process of HSA confirmed that the reaction of mild oxidants (Br2•−, N3•, SO4•−) with albumin leads to the formation of covalent bonds between tyrosine residues. In the case of •OH radicals and partly, Cl2•−, species other than DT are formed. The light emission of this species is similar to the emission of self-associated HSA.

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“…One of the methods of protein cross-linking is the formation of dityrosine bridges, which are formed as a result of the recombination of long-lived tyrosyl radicals (TyrO • ) generated under oxidative conditions. Our own study [ 4 ] and data presented in the literature [ 11 , 12 ] indicate that in aqueous solutions of tyrosine, TyrO • radicals are formed as one of the products of reaction with hydroxyl radicals. As a result of the reaction of • OH or

radicals with HSA molecules, stable protein aggregates of low and high molecular weight are formed.…”

Section: Resultsmentioning

confidence: 94%

Influence of Ionizing Radiation on Spontaneously Formed Aggregates in Proteins or Enzymes Solutions

Radomska

Wolszczak

2023

Pharmaceutics

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We have shown that many proteins and enzymes (ovalbumin, β-lactoglobulin, lysozyme, insulin, histone, papain) undergo concentration-dependent reversible aggregation as a result of the interaction of the studied biomolecules. Moreover, irradiation of those protein or enzyme solutions under oxidative stress conditions results in the formation of stable soluble protein aggregates. We assume that protein dimers are mainly formed. A pulse radiolysis study has been made to investigate the early stages of protein oxidation by N3• or •OH radicals. Reactions of the N3• radical with the studied proteins lead to the generation of aggregates stabilized by covalent bonds between tyrosine residues. The high reactivity of the •OH with amino acids contained within proteins is responsible for the formation of various covalent bonds (including C–C or C–O–C) between adjacent protein molecules. In the analysis of the formation of protein aggregates, intramolecular electron transfer from the tyrosine moiety to Trp• radical should be taken into account. Steady-state spectroscopic measurements with a detection of emission and absorbance, together with measurements of the dynamic scattering of laser light, made it possible to characterize the obtained aggregates. The identification of protein nanostructures generated by ionizing radiation using spectroscopic methods is difficult due to the spontaneous formation of protein aggregates before irradiation. The commonly used fluorescence detection of dityrosyl cross-linking (DT) as a marker of protein modification under the influence of ionizing radiation requires modification in the case of the tested objects. A precise photochemical lifetime measurement of the excited states of radiation-generated aggregates is useful in characterizing their structure. Resonance light scattering (RLS) has proven to be an extremely sensitive and useful technique to detect protein aggregates.

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A mechanistic approach towards the formation of bityrosine in proteins by ionizing radiation – GYG model peptide

Cited by 5 publications

References 36 publications

Strengthened Silk-Fibroin/Poly(ethylene oxide) Nonwoven Nanofibers: A Dual Green Process Using Pure Water for Electrospinning and Electron Beam-Assisted Cross-Linking

Strengthened Silk-Fibroin/Poly(ethylene oxide) Nonwoven Nanofibers: A Dual Green Process Using Pure Water for Electrospinning and Electron Beam-Assisted Cross-Linking

Spontaneous and Ionizing Radiation-Induced Aggregation of Human Serum Albumin: Dityrosine as a Fluorescent Probe

Influence of Ionizing Radiation on Spontaneously Formed Aggregates in Proteins or Enzymes Solutions

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