| Carboxymethylation of the fibrillar collagen with respect to formation of hydroxyapatite. | |
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MedLine Citation:
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PMID: 19957363 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Control over crystal growth by acidic matrix macromolecules is an important process in the formation of many mineralized tissues. Highly acidic macromolecules are postulated intermediates in tissue mineralization, because they sequester many calcium ions and occur in high concentrations at mineralizing foci in distantly related organisms. A prerequisite for biomineralization is the ability of cations like calcium to bind to proteins and to result in concert with appropriate anions like phosphates or carbonates in composite materials with bone-like properties. For this mineralization process the proteins have to be modified with respect to acidification. In this study we modified the protein collagen by carboxymethylation using glucuronic acid. Our experiments showed unambigously, that N(epsilon)-carboxymethyllysine is the major product of the in vitro nonenzymatic glycation reaction between glucuronic acid and collagen. We hypothesized that the function of biomimetically carboxymethylated collagen is to increase the local concentration of corresponding ions so that a critical nucleus of ions can be formed, leading to the formation of the mineral. Thus, the self-organization of HAP nanocrystals on and within collagen fibrils was intensified by carboxymethylation. |
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Authors:
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Hermann Ehrlich; Thomas Hanke; Paul Simon; Ren? Born; Christiane Fischer; Andrej Frolov; Tobias Langrock; Ralf Hoffmann; Uwe Schwarzenbolz; Thomas Henle; Vasily V Bazhenov; Hartmut Worch |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of biomedical materials research. Part B, Applied biomaterials Volume: 92 ISSN: 1552-4981 ISO Abbreviation: J. Biomed. Mater. Res. Part B Appl. Biomater. Publication Date: 2010 Feb |
Date Detail:
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Created Date: 2010-01-28 Completed Date: 2010-04-16 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101234238 Medline TA: J Biomed Mater Res B Appl Biomater Country: United States |
Other Details:
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Languages: eng Pagination: 542-51 Citation Subset: IM |
Affiliation:
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Institute of Bioanalytical Chemistry, TU Dresden, Dresden, 01069 Germany. Hermann.Ehrlich@tu-dresden.de |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Alkylation Amino Acids / analysis Biomimetics Borohydrides / chemistry Collagen / chemistry* Crystallization Glucose / chemistry Glucuronic Acid / chemistry Glyoxylates / chemistry Hydroxyapatites / chemistry* Indicators and Reagents Lysine / analogs & derivatives, chemistry Methylation Microfibrils Microscopy, Atomic Force Microscopy, Electron, Scanning Minerals / chemistry Spectroscopy, Fourier Transform Infrared |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/Borohydrides; 0/Glyoxylates; 0/Hydroxyapatites; 0/Indicators and Reagents; 0/Minerals; 25895-60-7/sodium cyanoborohydride; 298-12-4/glyoxylic acid; 50-99-7/Glucose; 56-87-1/Lysine; 5746-04-3/N(6)-carboxymethyllysine; 576-37-4/Glucuronic Acid; 9007-34-5/Collagen |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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