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 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.


DOI: 10.1101/2023.01.23.524231

Projects: Molecular Biomechanics

Publication type: Journal

Journal: biorxiv


Date Published: 23rd Jan 2023


Registered Mode: manually

Authors: Markus Kurth, Uladzimir Barayeu, Hassan Gharibi, Andrei Kuzhelev, Kai Riedmiller, Jennifer Zilke, Kasimir Noack, Vasyl Denysenkov, Reinhard Kappl, Thomas F. Prisner, Roman A. Zubarev, Tobias P. Dick, Frauke Gräter

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Kurth, M., Barayeu, U., Gharibi, H., Kuzhelev, A., Riedmiller, K., Zilke, J., Noack, K., Denysenkov, V., Kappl, R., Prisner, T. F., Zubarev, R. A., Dick, T. P., & Graeter, F. (2023). DOPA residues endow collagen with radical scavenging capacity. In []. Cold Spring Harbor Laboratory.

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Created: 24th Jan 2023 at 08:31

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