2021
DOI: 10.1016/j.radphyschem.2021.109644
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A mechanistic approach towards the formation of bityrosine in proteins by ionizing radiation – GYG model peptide

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Cited by 5 publications
(6 citation statements)
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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%
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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%
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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%
“…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%