Mechanoradicals in tensed tendon collagen as a source of oxidative stress
| Autor: | Vasyl Denysenkov, Uladzimir Barayeu, Marina Bennati, Csaba Daday, Agnieszka Obarska-Kosinska, Benedikt Rennekamp, Markus Kurth, Christopher Zapp, Tobias P. Dick, Frauke Gräter, David M. Hudson, Thomas F. Prisner, Davide Mercadante, Reinhard Kappl |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Biomaterials - proteins General Physics and Astronomy Biocompatible Materials medicine.disease_cause 01 natural sciences law.invention Tendons chemistry.chemical_compound Biopolymers law Hydrogen peroxide Electron paramagnetic resonance lcsh:Science chemistry.chemical_classification Condensed Matter - Materials Science Multidisciplinary Homolysis Dihydroxyphenylalanine Biological Physics (physics.bio-ph) Collagen Oxidation-Reduction Free Radicals Radical Science FOS: Physical sciences 010402 general chemistry General Biochemistry Genetics and Molecular Biology Article 03 medical and health sciences medicine Molecule Animals Physics - Biological Physics Biopolymers in vivo Bond cleavage Reactive oxygen species Electron Spin Resonance Spectroscopy Materials Science (cond-mat.mtrl-sci) General Chemistry 0104 chemical sciences Rats Oxidative Stress 030104 developmental biology chemistry Biophysics lcsh:Q Reactive Oxygen Species Oxidative stress |
| Zdroj: | Nature Communications, Vol 11, Iss 1, Pp 1-8 (2020) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | 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. The existence, nature and biological relevance of mechanoradicals in proteins are unknown. Here authors show that mechanical stress on collagen produces radicals and subsequently reactive oxygen species and suggest that collagen I evolved as a radical sponge against mechano-oxidative damage. |
| Databáze: | OpenAIRE |
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