ArticleJournal of structural biology2011
Self-aligning amelogenin nanoribbons in oil-water system.
Article in Journal of structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Human Enamel Formation: A Scoping Review for Oral Health Professionals.Dentistry journal · 2026Review
- Serine-16 Phosphorylation, C-Terminal Truncation, and Ion-Specific Interactions Coordinate Amelogenin Nanoribbon Formation.Calcified tissue international · 2026Article
- Amelogenin proteolysis orchestrates functional amyloid pathways in enamel development.Matrix biology : journal of the International Society for Matrix Biology · 2026Article
- Amyloid-induced mineralization: From biological systems to biomimetic materials.Bioactive materials · 2025Review
- High-yield recombinant bacterial expression ofProtein science : a publication of the Protein Society · 2023Article
- Residue-Specific Insights into the Intermolecular Protein-Protein Interfaces Driving Amelogenin Self-Assembly in Solution.Biochemistry · 2022Article
- Highly acidic pH facilitates enamel protein self-assembly, apatite crystal growth and enamel protein interactions in the early enamel matrix.Frontiers in physiology · 2022Article
- A Brief History of the Discovery of Amelogenin Nanoribbons In Vitro and In Vivo.Journal of dental research · 2021Article
- Mechanisms of Enamel Mineralization Guided by Amelogenin Nanoribbons.Journal of dental research · 2021Review
- Controls of nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite.Journal of structural biology · 2020Review
- Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin.International journal of molecular sciences · 2020Article
- Progression of Self-Assembly of Amelogenin Protein Supramolecular Structures in Simulated Enamel Fluid.Biomacromolecules · 2018Article
- Cloning and Expression Analysis of Human Amelogenin in Nicotiana benthamiana Plants by Means of a Transient Expression System.Molecular biotechnology · 2017Article
- Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Chemical Society reviews · 2017Review
- DENTAL ENAMEL FORMATION AND IMPLICATIONS FOR ORAL HEALTH AND DISEASE.Physiological reviews · 2017Review
- Amyloid-like ribbons of amelogenins in enamel mineralization.Scientific reports · 2016Article
- Materials engineering by ameloblasts.Journal of dental research · 2015Review
- Matching 4.7-Å XRD spacing in amelogenin nanoribbons and enamel matrix.Journal of dental research · 2014Article
- The proteolytic processing of amelogenin by enamel matrix metalloproteinase (MMP-20) is controlled by mineral ions.Biochimica et biophysica acta · 2013Article
- Self-assembly of filamentous amelogenin requires calcium and phosphate: from dimers via nanoribbons to fibrils.Biomacromolecules · 2012Article
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Authors and funding
5 authors.
Funding
Abstract
The highly organized microstructure of dental enamel is a result of protein-guided anisotropic growth of apatite nanofibers. It is established that amelogenin proteins, the main constituent of the developing enamel matrix, form nanospheres in vitro, but the amphiphilic nature of the full-length protein conveys the possibility of generating more complex structures as observed with other surfactant-like molecules. This study tested if the use of metastable oil-water emulsions can induce supramolecular assemblies of amelogenin. Recombinant full-length amelogenin, rH174, was mixed into octanol/ethyl acetate preparations of different ratios to form emulsions at pH 4.5 and 7.4. Atomic force and electron microscopy showed the formation of 16.7±1.0nm wide nanoribbons which grew to several micrometer length over a period of days. Nanoribbons formed from reverse micelles by enabling hydrophobic tails of the molecules to interact while preventing the formation of amelogenin nanospheres. Ribbon formation required the presence of calcium and phosphate ions and may be localized at a dark central line along the amelogenin ribbons. The ribbons have a strong tendency to align in parallel maintaining 5-20nm space between each other. The growth rates and number of ribbons were significantly higher at pH 4.5 and related to the metastability of the emulsion. A model for ribbon extension proposes the addition of short segments or amelogenin dimers to the ends of the ribbon. The formation of self-aligning and uniaxially elongating amelogenin structures triggered by the presence of calcium and phosphate may represent a suitable new model for protein controlled mineralization in enamel.
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