Progression of Self-Assembly of Amelogenin Protein Supramolecular Structures in Simulated Enamel Fluid

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Mechanisms of protein-guided mineralization in enamel, leading to organized fibrillar apatite nanocrystals, remain elusive. In vitro studies reveal recombinant human amelogenin (rH174), a matrix protein templating this process, self-assembles into a variety of structures. This study endeavors to clarify the self-assembly of rH174 in physiologically relevant conditions. Self-assembly in simulated enamel fluid was monitored up to 2 months. At alkali (7.3-8.7) and acidic (5.5-6.1) pH ranges, a distinct progression in formation was observed from nanospheres (17-23 nm) to intermediate-length nanorods, concluding with the formation of long 17-18 nm wide nanoribbons decorated with nanospheres. Assembly in acidic condition progressed quicker to nanoribbons with fewer persistent nanospheres. X-ray diffraction exhibited reflections characteristic of antiparallel β-sheets (4.7 and 9.65 Å), supporting the model of amyloid-like nanoribbon formation. This is the first observation of rH174 nanoribbons at alkaline pH as well as concurrent nanosphere formation, indicating both supramolecular structures are stable together under physiological conditions.


  • Sarah A Engelberth
  • Margot S Bacino
  • Shaiba Sandhu
  • Wu Li
  • Johan Bonde
  • Stefan Habelitz
Enheter & grupper
Externa organisationer
  • University of California, San Francisco

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Strukturbiologi
Sidor (från-till)3917-3924
Antal sidor8
Utgåva nummer10
StatusPublished - 2018
Peer review utfördJa