English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Mechanoradicals in tensed tendon collagen as a source of oxidative stress

Zapp, C., Obarska-Kosinska, A., Rennekamp, B., Kurth, M., Hudson, D. M., Mercadante, D., et al. (2020). Mechanoradicals in tensed tendon collagen as a source of oxidative stress. Nature Communications, 11: 2315. doi:10.1038/s41467-020-15567-4.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0006-A1EF-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0006-A21C-4
Genre: Journal Article

Files

show Files
hide Files
:
3240607.pdf (Publisher version), 2MB
Name:
3240607.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
:
3240607-Suppl.pdf (Supplementary material), 8MB
Name:
3240607-Suppl.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Zapp, C., Author
Obarska-Kosinska, A., Author
Rennekamp, B., Author
Kurth, M., Author
Hudson, D. M., Author
Mercadante, D., Author
Barayeu, U., Author
Dick, T. P., Author
Denysenkov, V., Author
Prisner, T., Author
Bennati, M.1, Author              
Daday, C., Author
Kappl, R., Author
Gräter, F., Author
Affiliations:
1Research Group of Electron Paramagnetic Resonance, MPI for Biophysical Chemistry, Max Planck Society, ou_578606              

Content

show
hide
Free keywords: Biomaterials – proteins; Biopolymers in vivo
 Abstract: As established nearly a century ago, mechanoradicals originate from homolytic bond scission in polymers. The existence, nature and biological relevance of mechanoradicals in proteins, instead, are unknown. We here show that mechanical stress on collagen produces radicals and subsequently reactive oxygen species, essential biological signaling molecules. Electron-paramagnetic resonance (EPR) spectroscopy of stretched rat tail tendon, atomistic molecular dynamics simulations and quantum-chemical calculations show that the radicals form by bond scission in the direct vicinity of crosslinks in collagen. Radicals migrate to adjacent clusters of aromatic residues and stabilize on oxidized tyrosyl radicals, giving rise to a distinct EPR spectrum consistent with a stable dihydroxyphenylalanine (DOPA) radical. The protein mechanoradicals, as a yet undiscovered source of oxidative stress, finally convert into hydrogen peroxide. Our study suggests collagen I to have evolved as a radical sponge against mechano-oxidative damage and proposes a mechanism for exercise-induced oxidative stress and redox-mediated pathophysiological processes.

Details

show
hide
Language(s): eng - English
 Dates: 2020-05-08
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41467-020-15567-4
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature Communications
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: 8 Volume / Issue: 11 Sequence Number: 2315 Start / End Page: - Identifier: -