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

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.

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 Creators:
Ehrlich, H., Author
Hanke, T., Author
Born, R., Author
Fischer, C., Author
Frolov, A., Author
Langrock, T., Author
Hoffmann, R., Author
Schwarzenbolz, U., Author
Henle, T., Author
Simon, P.1, Author           
Geiger, D., Author
Bazhenov, V. V., Author
Worch, H., Author
Affiliations:
1Paul Simon, Chemical Metal Science, Max Planck Institute for Chemical Physics of Solids, Max Planck Society, ou_1863418              

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Free keywords: Dual membrane diffusion system; Collagen; Carboxymethyllysine; Calcium phosphate phases
 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.

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Language(s): eng - English
 Dates: 2009
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 404359
ISI: 000263006500001
DOI: 10.1016/j.memsci.2008.10.003
 Degree: -

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Title: Journal of Membrane Science
  Alternative Title : J. Membr. Sci.
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 326 Sequence Number: - Start / End Page: 254 - 259 Identifier: ISSN: 0376-7388