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Intermolecular channels direct crystal orientation in mineralized collagen

Author

Listed:
  • YiFei Xu

    (Eindhoven University of Technology
    Eindhoven University of Technology
    University of Leeds)

  • Fabio Nudelman

    (Eindhoven University of Technology
    University of Edinburgh)

  • E. Deniz Eren

    (Eindhoven University of Technology
    Eindhoven University of Technology)

  • Maarten J. M. Wirix

    (Eindhoven University of Technology
    Eindhoven University of Technology)

  • Bram Cantaert

    (University of Leeds)

  • Wouter H. Nijhuis

    (Wilhelmina Children’s Hospital)

  • Daniel Hermida-Merino

    (DUBBLE@ESRF)

  • Giuseppe Portale

    (DUBBLE@ESRF
    University of Groningen)

  • Paul H. H. Bomans

    (Eindhoven University of Technology
    Eindhoven University of Technology)

  • Christian Ottmann

    (Eindhoven University of Technology
    Eindhoven University of Technology)

  • Heiner Friedrich

    (Eindhoven University of Technology
    Eindhoven University of Technology)

  • Wim Bras

    (DUBBLE@ESRF
    Oak Ridge National Laboratory)

  • Anat Akiva

    (Eindhoven University of Technology
    Eindhoven University of Technology
    Radboud University Medical Center)

  • Joseph P. R. O. Orgel

    (Illinois Institute of Technology)

  • Fiona C. Meldrum

    (University of Leeds)

  • Nico Sommerdijk

    (Eindhoven University of Technology
    Eindhoven University of Technology
    Radboud University Medical Center)

Abstract

The mineralized collagen fibril is the basic building block of bone, and is commonly pictured as a parallel array of ultrathin carbonated hydroxyapatite (HAp) platelets distributed throughout the collagen. This orientation is often attributed to an epitaxial relationship between the HAp and collagen molecules inside 2D voids within the fibril. Although recent studies have questioned this model, the structural relationship between the collagen matrix and HAp, and the mechanisms by which collagen directs mineralization remain unclear. Here, we use XRD to reveal that the voids in the collagen are in fact cylindrical pores with diameters of ~2 nm, while electron microscopy shows that the HAp crystals in bone are only uniaxially oriented with respect to the collagen. From in vitro mineralization studies with HAp, CaCO3 and γ-FeOOH we conclude that confinement within these pores, together with the anisotropic growth of HAp, dictates the orientation of HAp crystals within the collagen fibril.

Suggested Citation

  • YiFei Xu & Fabio Nudelman & E. Deniz Eren & Maarten J. M. Wirix & Bram Cantaert & Wouter H. Nijhuis & Daniel Hermida-Merino & Giuseppe Portale & Paul H. H. Bomans & Christian Ottmann & Heiner Friedric, 2020. "Intermolecular channels direct crystal orientation in mineralized collagen," Nature Communications, Nature, vol. 11(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18846-2
    DOI: 10.1038/s41467-020-18846-2
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    Cited by:

    1. Jinyuan Hu & Junhui Li & Jennifer Jiang & Lingling Wang & Jonathan Roth & Kenneth N. McGuinness & Jean Baum & Wei Dai & Yao Sun & Vikas Nanda & Fei Xu, 2022. "Design of synthetic collagens that assemble into supramolecular banded fibers as a functional biomaterial testbed," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    2. Marloes H. Bistervels & Balázs Antalicz & Marko Kamp & Hinco Schoenmaker & Willem L. Noorduin, 2023. "Light-driven nucleation, growth, and patterning of biorelevant crystals using resonant near-infrared laser heating," Nature Communications, Nature, vol. 14(1), pages 1-9, December.

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