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...

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Main Authors: Nair, Arun K., Gautieri, Alfonso, Chang, Shu-Wei, Buehler, Markus J.
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/
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