4.6 Article

Elastin-Like Protein, with Statherin Derived Peptide, Controls Fluorapatite Formation and Morphology

Journal

FRONTIERS IN PHYSIOLOGY
Volume 8, Issue -, Pages -

Publisher

FRONTIERS MEDIA SA
DOI: 10.3389/fphys.2017.00368

Keywords

enamel biomimetics; elastin-like proteins; fluorapatite; biomineralization model

Categories

Funding

  1. Life Science Initiative, QMUL
  2. European Research Council Starting Grant (STROFUNSCAFF)
  3. Marie Curie Career Integration Grant (BIOMORPH)
  4. EPSRC [EP/M022749/1]
  5. EPSRC [EP/L02263X/1, EP/M022749/1] Funding Source: UKRI
  6. Engineering and Physical Sciences Research Council [EP/L02263X/1, EP/M022749/1] Funding Source: researchfish

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.6
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available