Amelogenin and enamel biomimetics

Abstract

Mature tooth enamel is acellular and does not regenerate itself. Developing technologies that rebuild tooth enamel and preserve tooth structure is therefore of great interest. Considering the importance of amelogenin protein in dental enamel formation, its ability to control apatite mineralization in vitro, and its potential to be applied in fabrication of future bio-inspired dental material this review focuses on two major subjects: amelogenin and enamel biomimetics. We review the most recent findings on amelogenin secondary and tertiary structural properties with a focus on its interactions with different targets including other enamel proteins, apatite mineral, and phospholipids. Following a brief overview of enamel hierarchical structure and its mechanical properties we will present the state-of-the-art strategies in the biomimetic reconstruction of human enamel.

Repairing human tooth enamel with leucine-rich amelogenin peptide–chitosan hydrogel

“…Several strategies have been proposed to replicate the enamel microstructure using chemicals, polymers, amorphous calcium phosphate (ACP) nanoparticles, dendrimers, and hydrogels. 7 New approaches to enamel remineralization have included the use of b-sheet forming peptides, 8 electrospun mats of ACP/poly (vinylpyrrolidone) nanofibers, 9 amelogenin-releasing system, 10 and casein phosphopeptide stabilized ACP. 11 Yamagishi et al have developed a dental paste that upon application on the enamel surface, under acidic pH, resulted in the formation of organized nanocrystals of apatite.…”

State of the Art Enamel Remineralization Systems: The Next Frontier in Caries Management

“…Oral care products containing fluoride are effective in remineralizing enamel but do not have the potential to promote formation of organized apatite crystals [Ruan and Moradian-Oldak, 2015]. Presently, there is an attempt to shift from reparative to regenerative biomineralization therapies, wherein diseased dental tissues are replaced with biologically similar tissues [Alkilzy et al, 2018b].…”

“…However, mature enamel lacks matrix proteins and cannot regenerate the mineral loss caused by dental caries or erosion [Ruan and Moradian-Oldak, 2015]. Recently, several promising strategies have been proposed to replicate the complex enamel microstructure using synthetic amelogenin-based systems.…”

Intrinsically disordered proteins and biomineralization

“…Further, Wendy Shaw's group used NMR spectroscopy to examine the WT mouse and mutant amelogenins to confirm the pre-mature self-assembly of the mutant proteins [57]. Other studies show how the amelogenin structure is modified during its interaction with HA, phospholipids, other enamel proteins [58] and even collagen (remember that amelogenin does not interact with collagen in situ) [59] suggesting that during the complex interactions leading to HA formation other conformational changes are occurring.…”

“…The amelogenin molecules at pH 7.2 spontaneously self-assemble into oligomers and nanospheres. These subsequently bind together to form micro-ribbons [58]. Beniash et al suggest that this amelogenin self-assembly is attributable to formation of intramolecular hydrogen bonds between extended unordered regions of the protein, leading to the formation of tightly bound intrafibrillar β-strands [88].…”