In situ regeneration of the enamel-like structure of hydroxyapatite (HAp) crystals under oral conditions is significant for dental caries treatment. However, it is still a challenge for dentists to duplicate the elegant and well-aligned apatite structure bonding to the surface of demineralized enamel with traditional strategies such as fluoride treatment. Herein, we show a biocompatible amelogenin-inspired matrix, a phase-transited lysozyme (PTL) film mimicking a N-terminal amelogenin peptide with a central domain (N-Ame) combined with synthetic peptide (C-AMG) based on the functional domains of C-terminal telopeptide (C-Ame), which is formed by amyloid-like lysozyme aggregation at the enamel interface through a rapid one-step aqueous coating process. In the PTL/C-AMG matrix, C-AMG facilitated the oriented arrangement of amorphous calcium phosphate (ACP) nanoparticles and their transformation to ordered enamel-like HAp crystals, while PTL served as a strong interfacial anchor to immobilize the C-AMG and PTL/C-AMG matrix on verstaile substrate surfaces. PTL/C-AMG film-coated enamel induced the de novo synthesis of HAp crystals, facilitated epitaxial growth of HAp crystals and recovered the highly oriented structure and mechanical properties to levels nearly identical to those of natural enamel. This methodology of the bottom-up formation of enamel-like HAp crystals indicates that amyloid-like protein aggregates play a key role in the biomineralization of enamel mediated by amelogenin, providing a promising proof-of-concept strategy for treating early dental caries.

Dong Wang, Jingjing Deng, Xuliang Deng, Changqing Fang*, Xu Zhang*, Peng Yang*, Controlling Enamel Remineralization by Amyloid-like Amelogenin Mimics, Adv. Mater. 2020, 10.1002/adma.202002080, accepted.