Scientists Engineer Collagen to Neutralize Cell-Damaging Molecules
Researchers have modified collagen—a protein used in medical devices, cosmetics, and supplements—to actively scavenge harmful free radicals. The discovery could extend the shelf life of collagen products, reduce oxidative damage in wound healing applications, and open new markets for enhanced biomaterials across healthcare and consumer industries.
Originaltitel: DOPA Residues Endow Collagen with Radical Scavenging Capacity
Abstract 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.