ArticleEuropean journal of oral sciences2011
Self-assembly of amelogenin proteins at the water-oil interface.
Article in European journal of oral sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 22 citations in OpenAlex.
- 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-like amelogenin nanoribbons template mineralization via a low-energy interface of ion binding sites.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Protein nanoribbons template enamel mineralization.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- 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
- CaThe Journal of physiology · 2017Review
- Posttranslational Amelogenin Processing and Changes in Matrix Assembly during Enamel Development.Frontiers in physiology · 2017Article
- Dose-Dependent Rescue of KO Amelogenin Enamel by TransgenesFrontiers in physiology · 2017Article
- Amyloid-like ribbons of amelogenins in enamel mineralization.Scientific reports · 2016Article
- Sequence-Defined Energetic Shifts Control the Disassembly Kinetics and Microstructure of Amelogenin Adsorbed onto Hydroxyapatite (100).Langmuir : the ACS journal of surfaces and colloids · 2015Article
- 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
- Amelogenin and Enamel Biomimetics.Journal of materials chemistry. BArticle
- Truncated amelogenin and LRAP transgenes improve Amelx null mouse enamel.Matrix biology : journal of the International Society for Matrix BiologyArticle
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Self-assembly of amelogenin plays a key role in controlling enamel biomineralization. Recently, we generated self-aligning nanoribbons of amelogenin in water-in-oil emulsions stabilized by the full-length protein (rH174). Here, we tested the hypothesis that the hydrophilic C-terminus is critical for self-assembly of amelogenin into nanoribbons. The self-assembled structures of two amelogenin cleavage products, rH163 and rH146, were compared with structures of rH174 at different pH values and degrees of saturation using atomic force microscopy, electron microscopy, and dynamic light scattering. We observed that the number density of rH174 nanoribbons increased significantly when the initial pH was raised from 4.5 to 5.6. Nanoribbons, as well as unique helical nanostructures, were also readily observed when amelogenin rH146 was used, but showed little tendency for parallel alignment and did not bundle into fibrils like rH174. In contrast, rH163 rarely formed nanoribbons but predominantly assembled into nanospheres under the same conditions. We conclude that the presence of a hydrophilic C-terminus may not be a prerequisite for nanoribbon formation but may be critical for ribbon alignment and subsequent fibril formation. These results highlight the contribution of the hydrophobic domain in the self-assembly of elongated structures of amelogenins. Molecular mechanisms governing these processes based on the formation of reverse micelles are discussed.
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