ArticleThe journal of physical chemistry. C, Nanomaterials and interfaces2011
Partial high-resolution structure of phosphorylated and non-phosphorylated leucine-rich amelogenin protein adsorbed to hydroxyapatite.
Article in The journal of physical chemistry. C, Nanomaterials and interfaces, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
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Who cites it
20 citing papers in PubMed, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.
- Amelogenin-Derived Peptides in Bone Regeneration: A Systematic Review.International journal of molecular sciences · 2021Pooled it
- Effect of phosphate group on remineralization of early enamel caries regulated by amelogenin peptide.PloS one · 2024Article
- Molecular Cloning of Mouse Homologue of Enamel Protein C4orf26 and Its Phosphorylation by FAM20C.Calcified tissue international · 2021Article
- Binding Mode Characterization of Osteopontin on Hydroxyapatite by Solution NMR Spectroscopy.Chembiochem : a European journal of chemical biology · 2021Article
- Controls of nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite.Journal of structural biology · 2020Review
- Harnessing biomolecules for bioinspired dental biomaterials.Journal of materials chemistry. B · 2020Review
- Amelogenin phosphorylation regulates tooth enamel formation by stabilizing a transient amorphous mineral precursor.The Journal of biological chemistry · 2020Article
- Solid-State NMR and MD Study of the Structure of the Statherin Mutant SNa15 on Mineral Surfaces.Journal of the American Chemical Society · 2019Article
- Meeting report: a hard look at the state of enamel research.International journal of oral science · 2017Article
- Ubiquitin immobilized on mesoporous MCM41 silica surfaces - Analysis by solid-state NMR with biophysical and surface characterization.Biointerphases · 2017Article
- Protein Phosphorylation and Mineral Binding Affect the Secondary Structure of the Leucine-Rich Amelogenin Peptide.Frontiers in physiology · 2017Article
- Dynamic interactions of amelogenin with hydroxyapatite surfaces are dependent on protein phosphorylation and solution pH.Colloids and surfaces. B, Biointerfaces · 2016Article
- Solid-state NMR studies of proteins immobilized on inorganic surfaces.Solid state nuclear magnetic resonance · 2015Review
- The leucine-rich amelogenin protein (LRAP) is primarily monomeric and unstructured in physiological solution.Journal of structural biology · 2015Article
- The flexible structure of the K24S28 region of Leucine-Rich Amelogenin Protein (LRAP) bound to apatites as a function of surface type, calcium, mutation, and ionic strength.Frontiers in physiology · 2014Article
- Mineral association changes the secondary structure and dynamics of murine amelogenin.Journal of dental research · 2013Article
- Phosphorylation and ionic strength alter the LRAP-HAP interface in the N-terminus.Biochemistry · 2013Article
- Neutron reflectometry studies of the adsorbed structure of the amelogenin, LRAP.The journal of physical chemistry. B · 2013Article
- Using the RosettaSurface algorithm to predict protein structure at mineral surfaces.Methods in enzymology · 2013Review
- Amelogenin and Enamel Biomimetics.Journal of materials chemistry. BArticle
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The formation of biogenic materials requires the interaction of organic molecules with the mineral phase. In forming enamel, the amelogenin proteins contribute to the mineralization of hydroxyapatite (HAp). Leucine-rich amelogenin protein (LRAP) is a naturally occurring splice variant of amelogenin that comprises amelogenin's predicted HAp binding domains. We determined the partial structure of phosphorylated and non-phosphorylated LRAP variants bound to HAp using combined solid-state NMR (ssNMR) and ssNMR-biased computational structure prediction. New ssNMR measurements in the N-terminus indicate a largely extended structure for both variants, though some measurements are consistent with a partially helical N-terminal segment. The N-terminus of the phosphorylated variant is found to be consistently closer to the HAp surface than the non-phosphorylated variant. Structure prediction was biased using 21 ssNMR measurements in the N- and C-terminus at five HAp crystal faces. The predicted fold of LRAP is similar at all HAp faces studied, regardless of phosphorylation. Largely consistent with experimental observations, LRAP's predicted structure is relatively extended with a helix-turn-helix motif in the N-terminal domain and some helix in the C-terminal domain, and the N-terminal domain of the phosphorylated variant binds HAp more closely than the N-terminal domain of the non-phosphorylated variant. Predictions for both variants show some potential binding specificity for the {010} HAp crystal face, providing further support that amelogenins block crystal growth on the a and b faces to allow elongated crystals in the c-axis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.