English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons126855

Simon,  Paul
Paul Simon, Chemical Metal Science, Max Planck Institute for Chemical Physics of Solids, Max Planck Society;

/persons/resource/persons126692

Kniep,  Rüdiger
Rüdiger Kniep, Inorganic Chemistry, Max Planck Institute for Chemical Physics of Solids, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0027-F89B-9
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.