Abstract
AbstractHere 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.
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