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  Octacalcium phosphate - a metastable mineral phase controls the evolution of scaffold forming proteins

Pompe, W., Worch, H., Habraken, W. J. E. M., Simon, P., Kniep, R., Ehrlich, H., et al. (2015). Octacalcium phosphate - a metastable mineral phase controls the evolution of scaffold forming proteins. Journal of Materials Chemistry B, 3(26), 5318-5329. doi:10.1039/c5tb00673b.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-F89B-9 Version Permalink: http://hdl.handle.net/21.11116/0000-0001-1784-0
Genre: Journal Article

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 Creators:
Pompe, Wolfgang1, Author
Worch, Hartmut1, Author
Habraken, Wouter J. E. M.1, Author
Simon, Paul2, Author              
Kniep, Rüdiger3, Author              
Ehrlich, Hermann1, Author
Paufler, Peter1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Paul Simon, Chemical Metal Science, Max Planck Institute for Chemical Physics of Solids, Max Planck Society, ou_1863418              
3Rüdiger Kniep, Inorganic Chemistry, Max Planck Institute for Chemical Physics of Solids, Max Planck Society, ou_1863437              

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 Abstract: The molecular structure of collagen type 1 can be understood as the result of evolutionary selection in the process of formation of calcium phosphate based biocomposites acting as load bearing components in living organisms. The evolutionary selection fulfills the principle of 'survival of the fittest' in a particular biological environment. Disk-like post-nucleation complexes of Ca-2(HPO4)(3)(2-) organized in ribbon-like assemblies in the metastable octacalcium phosphate (OCP) phase, and Ca-3 triangles in the stable HAP phase had formed the crystallographic motifs in this selection process. The rotational as well as the translational symmetry of the major tropocollagen (TC) helix agree nearly perfectly with the corresponding symmetries of the OCP structure. The sequence of (Gly-X-Y) motifs of the three a chains constituting the TC molecule enables an optimized structural fit for the nucleation of Ca-3 triangles, the directed growth of nanostructured OCP, and the subsequent formation of hydroxyapatite (HAP) in collagen macrofibrils by a topotaxial transition. The known connection between genetic defects of collagen type 1 and Osteogenesis imperfecta should motivate the search for similar dependences of other bone diseases on a disturbed molecular structure of collagen on the genetic scale.

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Language(s): eng - English
 Dates: 2015-06-282015-06-28
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000356964700022
DOI: 10.1039/c5tb00673b
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Title: Journal of Materials Chemistry B
Source Genre: Journal
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Publ. Info: Cambridge, UK : Royal Society of Chemistry
Pages: - Volume / Issue: 3 (26) Sequence Number: - Start / End Page: 5318 - 5329 Identifier: ISSN: 2050-750X
CoNE: /journals/resource/2050-750X