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Primary radiation damage in bone evolves via collagen destruction by photoelectrons and secondary emission self-absorption

Author

Listed:
  • Katrein Sauer

    (Charité – Universitätsmedizin Berlin, Department for Operative, Preventive and Pediatric Dentistry)

  • Ivo Zizak

    (Department for Structure and Dynamics of Energy Materials (SE-ASD))

  • Jean-Baptiste Forien

    (Materials Science Division)

  • Alexander Rack

    (ESRF - The European Synchrotron)

  • Ernesto Scoppola

    (Department of Biomaterials)

  • Paul Zaslansky

    (Charité – Universitätsmedizin Berlin, Department for Operative, Preventive and Pediatric Dentistry)

Abstract

X-rays are invaluable for imaging and sterilization of bones, yet the resulting ionization and primary radiation damage mechanisms are poorly understood. Here we monitor in-situ collagen backbone degradation in dry bones using second-harmonic-generation and X-ray diffraction. Collagen breaks down by cascades of photon-electron excitations, enhanced by the presence of mineral nanoparticles. We observe protein disintegration with increasing exposure, detected as residual strain relaxation in pre-stressed apatite nanocrystals. Damage rapidly grows from the onset of irradiation, suggesting that there is no minimal ‘safe’ dose that bone collagen can sustain. Ionization of calcium and phosphorous in the nanocrystals yields fluorescence and high energy electrons giving rise to structural damage that spreads beyond regions directly illuminated by the incident radiation. Our findings highlight photoelectrons as major agents of damage to bone collagen with implications to all situations where bones are irradiated by hard X-rays and in particular for small-beam mineralized collagen fiber investigations.

Suggested Citation

  • Katrein Sauer & Ivo Zizak & Jean-Baptiste Forien & Alexander Rack & Ernesto Scoppola & Paul Zaslansky, 2022. "Primary radiation damage in bone evolves via collagen destruction by photoelectrons and secondary emission self-absorption," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34247-z
    DOI: 10.1038/s41467-022-34247-z
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    References listed on IDEAS

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    1. Stéphane Bancelin & Carole Aimé & Ivan Gusachenko & Laura Kowalczuk & Gaël Latour & Thibaud Coradin & Marie-Claire Schanne-Klein, 2014. "Determination of collagen fibril size via absolute measurements of second-harmonic generation signals," Nature Communications, Nature, vol. 5(1), pages 1-8, December.
    2. Admir Masic & Luca Bertinetti & Roman Schuetz & Shu-Wei Chang & Till Hartmut Metzger & Markus J. Buehler & Peter Fratzl, 2015. "Osmotic pressure induced tensile forces in tendon collagen," Nature Communications, Nature, vol. 6(1), pages 1-8, May.
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