English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

On the Function of Saccharides during the Nucleation of Calcium Carbonate-Protein Biocomposites

MPS-Authors
/persons/resource/persons126590

Duchstein,  P.
Max Planck Institute for Chemical Physics of Solids, Max Planck Society;

/persons/resource/persons126692

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

/persons/resource/persons126922

Zahn,  D.
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

Duchstein, P., Kniep, R., & Zahn, D. (2013). On the Function of Saccharides during the Nucleation of Calcium Carbonate-Protein Biocomposites. Crystal Growth & Design, 13(11), 4885-4889. doi:10.1021/cg401070h.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0015-1E24-E
Abstract
The molecular mechanism of calcium carbonate nucleation in the presence of various types of collageneous proteins is unravelled from computer simulation of ion-by-ion association steps. Single calcium ions are incorporated in the triplehelix by formation of salt bridges to carbonyl and hydroxyl groups of collagen, while single carbonate ions tend to bind laterally to the biomolecule. However, upon multiple ion association, the self-organization of the forming aggregate strongly depends on the triple-helical collagenous strand. In absence of glycosylated lysine residues, we observed that carbonate ions bind to calcium ions that are already incorporated into the triple helix and eventually cause the unfolding of the protein. On the other hand, otolin-1, a specific, collagen-like protein found in biogenic calcite-based composites such as otoconia, comprises a particularly high degree of glycosylated amino acids which avoid such "destructive" calcium carbonate contacts by providing alternative association sites more lateral to the backbone. This leads to the formation of a saccharide calcium carbonate agglomerate that does not compromise the protein's triple helix and constitutes the organic inorganic interface of the nucleating biocomposite.