English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Mineralization of biomimetically carboxymethylated collagen fibrils in a model dual membrane diffusion system

MPS-Authors
/persons/resource/persons126855

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

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Ehrlich, H., Hanke, T., Born, R., Fischer, C., Frolov, A., Langrock, T., et al. (2009). Mineralization of biomimetically carboxymethylated collagen fibrils in a model dual membrane diffusion system. Journal of Membrane Science, 326, 254-259. doi:10.1016/j.memsci.2008.10.003.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0015-2596-4
Abstract
In the present work, we show for the first time, that N-epsilon-carboxymethyllysine is the major product of the in vitro non-enzymatic glycation reaction between fibrillar collagen and glucuronic acid. Dual diffusion membrane system was effectively used for oriented crystal growth of octacalcium phosphate/hydroxyapatite on the biomimetically carboxymethylated collagen fibrils. We hypothesize that the function of biomimetically carboxymethylated collagen is to increase the local concentration of corresponding ions in such a way that a critical nucleus of ions can be formed, leading to the formation of the mineral under specific micro-environment conditions achieved by using diffusion membrane system. (c) 2008 Elsevier B.V. All rights reserved.