Self-assembly and effect on crystal growth of the leucine-rich amelogenin peptide.

@article{Habelitz2006SelfassemblyAE,
  title={Self-assembly and effect on crystal growth of the leucine-rich amelogenin peptide.},
  author={Stefan Habelitz and Pamela K Denbesten and Sally Jean Marshall and Grayson William Marshall and Wu Li},
  journal={European journal of oral sciences},
  year={2006},
  volume={114 Suppl 1},
  pages={315-9; discussion 327-9, 382}
}
Amelogenins are a unique group of alternatively spliced proteins. While the full-length amelogenin is known to assemble into nanospheres and alter apatite crystal growth and alignment, the function of the leucine-rich amelogenin peptide (LRAP) in biomineralization is not understood. This study tested the hypothesis that LRAP self-assembles into a supramolecular structure and guides crystal growth similarly to the full-length protein. Synthetic LRAP and recombinant full-length amelogenin (rH175… CONTINUE READING