| Polyelectrolyte-mediated adsorption of amelogenin monomers and nanospheres forming mono- or multilayers. | |
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MedLine Citation:
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PMID: 17579474 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We have applied optical waveguide lightmode spectroscopy combined with streaming potential measurements and Fourier-transformed infrared spectroscopy to investigate adsorption of amelogenin nanospheres onto polyelectrolytes. The long-term objective was to better understand the chemical nature of these assemblies and to gain further insight into the molecular mechanisms involved during self-assembly. It was found that monolayers of monomers and negatively charged nanospheres of a recombinant amelogenin (rM179) irreversibly adsorbed onto a positively charged polyelectrolyte multilayer films. On the basis of measurements performed at different temperatures, it was demonstrated that intermolecular interactions for the formation of nanospheres were not affected by their adsorption onto polyelectrolytes. Consecutive adsorption of nanospheres resulting in the formation of multilayer structures was possible by using cationic poly(l-lysine) as mediators. N-Acetyl-d-glucosamine (GlcNac) did not disturb the nanosphere-assembled protein's structure, and it only affected the adsorption of monomeric amelogenin. Infrared spectroscopy of adsorbed amelogenin revealed conformational differences between the monomeric and assembled forms of rM179. While there was a considerable amount of alpha-helices in the monomers, beta-turn and beta-sheet structures dominated the assembled proteins. Our work constitutes the first report on a structurally controlled in vitro buildup of an rM179 nanosphere monolayer-based matrix. Our data support the notion that amelogenin self-assembly is mostly driven by hydrophobic interactions and that amelogenin/PEM interactions are dominated by electrostatic forces. We suggest that similar forces can govern amelogenin interactions with non-amelogenins or the mineral phase during enamel biomineralization. |
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Authors:
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Csilla Gergely; Balazs Szalontai; Janet Moradian-Oldak; Frédéric J G Cuisinier |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2007-06-19 |
Journal Detail:
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Title: Biomacromolecules Volume: 8 ISSN: 1525-7797 ISO Abbreviation: Biomacromolecules Publication Date: 2007 Jul |
Date Detail:
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Created Date: 2007-07-09 Completed Date: 2007-10-25 Revised Date: 2012-10-09 |
Medline Journal Info:
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Nlm Unique ID: 100892849 Medline TA: Biomacromolecules Country: United States |
Other Details:
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Languages: eng Pagination: 2228-36 Citation Subset: IM |
Affiliation:
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Groupe d'étude des Semi-Conducteurs, Université Montpellier II, Montpellier Cedex 5, France. gergely@ges.univ-montp2.fr |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adsorption Amelogenin / chemistry* Amino Acid Sequence Animals Electrolytes / chemistry* Mice Molecular Sequence Data Nanotubes* Spectroscopy, Fourier Transform Infrared |
| Grant Support | |
ID/Acronym/Agency:
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DE013414/DE/NIDCR NIH HHS; DE015332-01/DE/NIDCR NIH HHS; R01 DE013414-06/DE/NIDCR NIH HHS; R01 DE020099/DE/NIDCR NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Amelogenin; 0/Electrolytes |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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