DOPA Residues Endow Collagen with Radical Scavenging Capacity

Here we uncover collagen, the main structural protein of all connective tissues, as a redox‐active material. We identify dihydroxyphenylalanine (DOPA) residues, post‐translational oxidation products of tyrosine residues, to be common in collagen derived from different connective tissues. We observe...

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Bibliographic Details
Published in:Angewandte Chemie 2023-06, Vol.135 (24), p.n/a
Main Authors: Kurth, Markus, Barayeu, Uladzimir, Gharibi, Hassan, Kuzhelev, Andrei, Riedmiller, Kai, Zilke, Jennifer, Noack, Kasimir, Denysenkov, Vasyl, Kappl, Reinhard, Prisner, Thomas F., Zubarev, Roman A., Dick, Tobias P., Gräter, Frauke
Format: Article
Language:English
Subjects:
Amino acids
Ascorbic acid
Chemistry
Collagen
Connective tissues
Dihydroxyphenylalanine
Hydrogen peroxide
Oxidation
Peroxides
Quinones
Radicals
Redox Chemistry
Residues
Scavenging
Tyrosine
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Summary:Here we uncover collagen, the main structural protein of all connective tissues, as a redox‐active material. We identify dihydroxyphenylalanine (DOPA) residues, post‐translational oxidation products of tyrosine residues, to be common in collagen derived from different connective tissues. We observe that these DOPA residues endow collagen with substantial radical scavenging capacity. When reducing radicals, DOPA residues work as redox relay: they convert to the quinone and generate hydrogen peroxide. In this dual function, DOPA outcompetes its amino acid precursors and ascorbic acid. Our results establish DOPA residues as redox‐active side chains of collagens, probably protecting connective tissues against radicals formed under mechanical stress and/or inflammation. Peptide‐bound dihydroxyphenylalanine (DOPA) is a component of tendon and meniscus tissue and originates from tyrosine oxidation. Both in situ and in vitro, DOPA proved to be a highly efficient radical scavenger, with the products of radical degradation being hydrogen peroxide and DOPA quinone. Thus, we suggest that the DOPA pathway is part of a tissue‐inherent redox buffer system.
ISSN:0044-8249
1521-3757
DOI:10.1002/ange.202216610