Enamel is a hard nanocomposite bioceramic with significant resilience that protects the mammalian tooth from external physical and chemical damages. The remarkable mechanical properties of enamel are associated with its hierarchical structural organization and its thorough connection with underlying dentin. This dynamic mineralizing system offers scientists a wealth of information that allows the study of basic principels of organic matrix-mediated biomineralization and can potentially be utilized in the fields of material science and engineering for development and design of biomimetic materials. This chapter will provide a brief overview of enamel hierarchical structure and properties and the process and stages of amelogenesis. Particular emphasis is given to current knowledge of extracellular matrix protein and proteinases, and the structural chemistry of the matrix components and their putative functions. The chapter will conclude by discussing the potential of enamel for regrowth.
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.
Biomineralization of enamel, dentin, and bone involves the deposition of apatite mineral crystals within an organic matrix. Bone and teeth are classic examples of biomaterials with unique biomechanical properties that are crucial to their function. The collagen-based apatite mineralization and the important function of noncollagenous proteins are similar in dentin and bone; however, enamel is formed in a unique amelogenin-containing protein matrix. While the structure and organic composition of enamel are different from those of dentin and bone, the principal molecular mechanisms of protein–protein interactions, protein self-assembly, and control of crystallization events by the organic matrix are common among these apatite-containing tissues. This review briefly summarizes enamel and dentin matrix components and their interactions with other extracellular matrix components and calcium ions in mediating the mineralization process. We highlight the crystallization events that are controlled by the protein matrix and their interactions in the extracellular matrix during enamel and dentin biomineralization. Strategies for peptide-inspired biomimetic growth of tooth enamel and bioinspired mineralization of collagen to stimulate repair of demineralized dentin and bone tissue engineering are also addressed.