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• W2621871842 abstract "The process of enamel biomineralization is multi-step, complex and mediated by organic molecules. The lack of cells in mature enamel leaves it unable to regenerate and hence novel ways of growing enamel-like structures are currently being investigated. Recently, elastin-like protein (ELP) with the analog N-terminal sequence of statherin (STNA15-ELP) has been used to regenerate mineralized tissue. Here, the STNA15-ELP has been mineralized in constrained and unconstrained conditions in a fluoridated solution. We demonstrate that the control of STNA15-ELP delivery to the mineralizing solution can form layered ordered fluorapatite mineral, via a brushite precursor. We propose that the use of a constrained STNA15-ELP system can lead to the development of novel, bioinspired enamel therapeutics." @default.
• W2621871842 created "2017-06-15" @default.
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• W2621871842 date "2017-06-08" @default.
• W2621871842 modified "2023-10-13" @default.
• W2621871842 title "Elastin-Like Protein, with Statherin Derived Peptide, Controls Fluorapatite Formation and Morphology" @default.
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• W2621871842 doi "https://doi.org/10.3389/fphys.2017.00368" @default.
• W2621871842 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5462913" @default.
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