Document Detail


Carboxymethylation of the fibrillar collagen with respect to formation of hydroxyapatite.
MedLine Citation:
PMID:  19957363     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
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:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
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:
Created Date:  2010-01-28     Completed Date:  2010-04-16     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101234238     Medline TA:  J Biomed Mater Res B Appl Biomater     Country:  United States    
Other Details:
Languages:  eng     Pagination:  542-51     Citation Subset:  IM    
Affiliation:
Institute of Bioanalytical Chemistry, TU Dresden, Dresden, 01069 Germany. Hermann.Ehrlich@tu-dresden.de
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MeSH Terms
Descriptor/Qualifier:
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:
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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