DOPA Residues Endow Collagen with Radical Scavenging Capacity.
Angew Chem Int Ed Engl
; 62(24): e202216610, 2023 06 12.
Article
em En
| MEDLINE
| ID: mdl-37009775
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.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Tirosina
/
Di-Hidroxifenilalanina
Idioma:
En
Ano de publicação:
2023
Tipo de documento:
Article