Enamel biomineralization: A multi-disciplined approach to understand a natural protein-mineral interface. Year 3.
EMSL Project ID
50110
Abstract
Aamelogenin is the central protein controlling the formation of dental enamel, the hardest tissue in the human body. It orchestrates the nucleation, growth, and organization of enamel (amelogenesis) through the formation of large quaternary structures called nanospheres, consisting of 20-100 monomers. Amelogenin orchestrates the nucleation, growth, and organization of enamel formation (amelogenesis) after its initial conformation of large oligomeric structures called nanospheres, consisting of 20-100 monomers. Documenting the conformational details and how the structure spearheads the structure and function of full-length murine amelogenin (M179) through-out the process of enamel formation is the focus of our five-year, NIH funded investigations. With FY18 representsing the third year of our project and, therefore some of thenumerous experiments such as liquid- and solid- state NMR experiments having been completed, structural assignments and some of the rigid-solid state protein identification experiments are underway and are being incorporated in papers under construction. We request follow-on EMSL resources to accomplish tasks which requirewe realize the need for superior equipment to fully elucidate the amelogenin quaternary structure before and after association with the mineral surface. Current Recent data with residue-specific 13C-, 15N-labeled samples on a mineral surface support the a structure arrangements leading tocomposed of anti-parallel arrays as proposed by Beniash et al. (PNAS, 108:34, 2011) which exists in the mineralized protein sample. To verify such a structure, increased sensitivity and resolution afforded by the collection of data on a fully 13C-, 15N-labeled using a High Resolution Magic Angle Spinning (HRMAS) probe is required. HRMAS access highlight the first of our three experimental aims in FY18 that require access to EMSL resources.
Project Details
Start Date
2017-12-20
End Date
2018-09-30
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members
Related Publications
Buchko G.W., R.M. Jayasinha Arachchige, J. Tao, B.J. Tarasevich, and W.J. Shaw. 2018. "Identification of major metalloproteinase-20 proteolytic processing products of murine amelogenin and tyrosine-rich amleogenin peptide using a nuclear magnetic resonance spectroscopy based method." Archives of Oral Biology 93, no. 1:187-194. PNNL-SA-132678. doi:10.1016/j.archoralbio.2018.06.001
Jayasinha Arachchige R.M., S.D. Burton, J. Lu, B. Ginovska, L.K. Harding, M.E. Taylor, and J. Tao, et al. 2018. "Solid-State NMR Identification of Intermolecular Interactions in Amelogenin Bound to Hydroxyapatite." Biophysical Journal 115, no. 9:1666-1672. PNNL-SA-131727. doi:10.1016/j.bpj.2018.08.027
Tao J., Y. Shin, R.M. Jayasinha Arachchige, G.W. Buchko, S.D. Burton, A. Dohnalkova, and Z. Wang, et al. 2019. "The energetic basis for hydroxyapatite mineralization by amelogenin variants provides insights into the origin of amelogenesis imperfecta." Proceedings of the National Academy of Sciences of the United States of America 116, no. 28:13867-13872. PNNL-SA-143391. doi:10.1073/pnas.1815654116