ArticleProceedings of the National Academy of Sciences of the United States of America2022
Amyloid-like amelogenin nanoribbons template mineralization via a low-energy interface of ion binding sites.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Bioinstructive Orthogonally-crosslinked Ovoprotein Microgels for Modular Bioprinting.bioRxiv : the preprint server for biology · 2026Article
- 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
- The Role of Confinement in Biomineralization.Chemical reviews · 2025Review
- Amyloid-induced mineralization: From biological systems to biomimetic materials.Bioactive materials · 2025Review
- Mesoscale orchestration of collagen-based hierarchical mineralization.Nature communications · 2025Article
- Unraveling α-synuclein and amylin co-aggregation: pathological insights and biomarker development for Parkinson's disease.Theranostics · 2025Article
- A polymer deposition-mediated surface-charge reformation strategy: reversing the MOF biomineralization behavior.Chemical science · 2024Article
- Amyloid and collagen templates in aortic valve calcification.Trends in molecular medicine · 2024Article
- Implementing reactivity in molecular dynamics simulations with harmonic force fields.Nature communications · 2024Article
- VMT/ACP/Dextran composite nanosheets against dental caries through promoting mineralization of dentin tubules, pH buffering, and antibacterial.Journal of nanobiotechnology · 2024Article
- Kinetics of Calcite Nucleation onto Sulfated Chitosan Derivatives and Implications for Water-Polysaccharide Interactions during Crystallization of Sparingly Soluble Salts.Crystal growth & design · 2024Article
- De novo design of pH-responsive self-assembling helical protein filaments.Nature nanotechnology · 2024Article
- New Nano-Crystalline Hydroxyapatite-Polycarboxy/Sulfo Betaine Hybrid Materials: Synthesis and Characterization.Molecules (Basel, Switzerland) · 2024Article
- The contribution of amyloid deposition in the aortic valve to calcification and aortic stenosis.Nature reviews. Cardiology · 2023Review
- Resolving protein-mineral interfacial interactions duringMaterials today. Advances · 2023Article
- Biomimetic Mineral Synthesis by Nanopatterned Supramolecular-Block Copolymer Templates.Nano letters · 2023Article
- Calcium interactions in amelogenin-derived peptide assembly.Frontiers in physiology · 2022Article
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Authors and funding
10 authors.
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Abstract
Protein scaffolds direct the organization of amorphous precursors that transform into mineralized tissues, but the templating mechanism remains elusive. Motivated by models for the biomineralization of tooth enamel, wherein amyloid-like amelogenin nanoribbons guide the mineralization of apatite filaments, we investigated the impact of nanoribbon structure, sequence, and chemistry on amorphous calcium phosphate (ACP) nucleation. Using full-length human amelogenin and peptide analogs with an amyloid-like domain, films of β-sheet nanoribbons were self-assembled on graphite and characterized by in situ atomic force microscopy and molecular dynamics simulations. All sequences substantially reduce nucleation barriers for ACP by creating low-energy interfaces, while phosphoserines along the length of the nanoribbons dramatically enhance kinetic factors associated with ion binding. Furthermore, the distribution of negatively charged residues along the nanoribbons presents a potential match to the Ca–Ca distances of the multi-ion complexes that constitute ACP. These findings show that amyloid-like amelogenin nanoribbons provide potent scaffolds for ACP mineralization by presenting energetically and stereochemically favorable templates of calcium phosphate ion binding and suggest enhanced surface wetting toward calcium phosphates in general.
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