Shuturminska, K, Tarakina, NV, Azevedo, HS et al. (4 more authors) (2017) Elastin-Like Protein, with Statherin Derived Peptide, Controls Fluorapatite Formation and Morphology. Frontiers in Physiology, 8. 368. ISSN 1664-042X
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2017 Shuturminska, Tarakina, Azevedo, Bushby, Mata, Anderson and Al-Jawad. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
Keywords: | enamel biomimetics, elastin-like proteins, fluorapatite, biomineralization model |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Medicine and Health (Leeds) > School of Dentistry (Leeds) > Oral Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 10 Feb 2020 11:14 |
Last Modified: | 10 Feb 2020 11:14 |
Status: | Published |
Publisher: | Frontiers Media |
Identification Number: | 10.3389/fphys.2017.00368 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:156769 |