Molecular mechanics of mineralized collagen fibrils in bone
Bone is a natural composite of collagen protein and the mineral hydroxyapatite. The structure of bone is known to be important to its load-bearing characteristics, but relatively little is known about this structure or the mechanism that govern deformation at the molecular scale. Here we perform ful...
Main Authors: | , , , |
---|---|
Format: | Online |
Language: | English |
Published: |
Nature Pub. Group
2013
|
Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3644085/ |
id |
pubmed-3644085 |
---|---|
recordtype |
oai_dc |
spelling |
pubmed-36440852013-05-17 Molecular mechanics of mineralized collagen fibrils in bone Nair, Arun K. Gautieri, Alfonso Chang, Shu-Wei Buehler, Markus J. Article Bone is a natural composite of collagen protein and the mineral hydroxyapatite. The structure of bone is known to be important to its load-bearing characteristics, but relatively little is known about this structure or the mechanism that govern deformation at the molecular scale. Here we perform full-atomistic calculations of the three-dimensional molecular structure of a mineralized collagen protein matrix to try to better understand its mechanical characteristics under tensile loading at various mineral densities. We find that as the mineral density increases, the tensile modulus of the network increases monotonically and well beyond that of pure collagen fibrils. Our results suggest that the mineral crystals within this network bears up to four times the stress of the collagen fibrils, whereas the collagen is predominantly responsible for the material’s deformation response. These findings reveal the mechanism by which bone is able to achieve superior energy dissipation and fracture resistance characteristics beyond its individual constituents. Nature Pub. Group 2013-04-16 /pmc/articles/PMC3644085/ /pubmed/23591891 http://dx.doi.org/10.1038/ncomms2720 Text en Copyright © 2013, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. http://creativecommons.org/licenses/by-nc-sa/3.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/ |
repository_type |
Open Access Journal |
institution_category |
Foreign Institution |
institution |
US National Center for Biotechnology Information |
building |
NCBI PubMed |
collection |
Online Access |
language |
English |
format |
Online |
author |
Nair, Arun K. Gautieri, Alfonso Chang, Shu-Wei Buehler, Markus J. |
spellingShingle |
Nair, Arun K. Gautieri, Alfonso Chang, Shu-Wei Buehler, Markus J. Molecular mechanics of mineralized collagen fibrils in bone |
author_facet |
Nair, Arun K. Gautieri, Alfonso Chang, Shu-Wei Buehler, Markus J. |
author_sort |
Nair, Arun K. |
title |
Molecular mechanics of mineralized collagen fibrils in bone |
title_short |
Molecular mechanics of mineralized collagen fibrils in bone |
title_full |
Molecular mechanics of mineralized collagen fibrils in bone |
title_fullStr |
Molecular mechanics of mineralized collagen fibrils in bone |
title_full_unstemmed |
Molecular mechanics of mineralized collagen fibrils in bone |
title_sort |
molecular mechanics of mineralized collagen fibrils in bone |
description |
Bone is a natural composite of collagen protein and the mineral hydroxyapatite. The structure of bone is known to be important to its load-bearing characteristics, but relatively little is known about this structure or the mechanism that govern deformation at the molecular scale. Here we perform full-atomistic calculations of the three-dimensional molecular structure of a mineralized collagen protein matrix to try to better understand its mechanical characteristics under tensile loading at various mineral densities. We find that as the mineral density increases, the tensile modulus of the network increases monotonically and well beyond that of pure collagen fibrils. Our results suggest that the mineral crystals within this network bears up to four times the stress of the collagen fibrils, whereas the collagen is predominantly responsible for the material’s deformation response. These findings reveal the mechanism by which bone is able to achieve superior energy dissipation and fracture resistance characteristics beyond its individual constituents. |
publisher |
Nature Pub. Group |
publishDate |
2013 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3644085/ |
_version_ |
1611975189663318016 |