A biomimetic model for mineralization of type-I collagen fibrils

Shasha Yao, Yifei Xu, Changyu Shao, Fabio Nudelman, Nico A.J.M. Sommerdijk, Ruikang Tang

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

Abstract

The bone and dentin mainly consist of type-I collagen fibrils mineralized by hydroxyapatite (HAP) nanocrystals. In vitro biomimetic models based on self-assembled collagen fibrils have been widely used in studying the mineralization mechanism of type-I collagen. In this chapter, the protocol we used to build a biomimetic model for the mechanistic study of type-I collagen mineralization is described. Type-I collagen extracted from rat tail tendon or horse tendon is self-assembled into fibrils and mineralized by HAP in vitro. The mineralization process is monitored by cryoTEM in combination with two-dimensional (2D) and three-dimensional (3D) stochastic optical reconstruction microscopy (STORM), which enables in situ and high-resolution visualization of the process.

Original languageEnglish
Title of host publicationCollagen
Subtitle of host publicationMethods and protocols
EditorsIrit Sagi, Nikolaos A. Afratis
PublisherSpringer
Pages39-54
Number of pages16
ISBN (Electronic)978-1-4939-9095-5
ISBN (Print)978-1-2939-9094-8
DOIs
Publication statusPublished - 1 Jan 2019

Publication series

NameMethods in Molecular Biology
PublisherHumana Press
Volume1944
ISSN (Print)1064-3745

Keywords

  • Bone
  • Calcium phosphate
  • CryoTEM
  • STORM
  • Type-I collagen

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  • Cite this

    Yao, S., Xu, Y., Shao, C., Nudelman, F., Sommerdijk, N. A. J. M., & Tang, R. (2019). A biomimetic model for mineralization of type-I collagen fibrils. In I. Sagi, & N. A. Afratis (Eds.), Collagen: Methods and protocols (pp. 39-54). (Methods in Molecular Biology; Vol. 1944). Springer. https://doi.org/10.1007/978-1-4939-9095-5_4