A Critical Survey of Biomineralization: Control, Mechanisms, by Jürgen Engel

By Jürgen Engel

This monograph presents a accomplished and updated process on biomineralization. The topical concentration of the e-book lies at the query of the way matrix proteins and cells catalyze and keep an eye on mineralization in organisms. fresh advances within the knowing of biomineralization aid to higher comprehend biomaterials, particularly their mechanical houses. the objective viewers essentially contains practitioners and learn specialists within the box, however the publication can also be invaluable for graduate scholars.

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Extra resources for A Critical Survey of Biomineralization: Control, Mechanisms, Functions and Material Properties

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By electron microscopy, organic material in the enamel region has been observed and interpreted as an amelogenin matrix. In addition, an electron microscopically visible “cover” on the enamel rods has been interpreted as an ameloblastin layer [9]. Both interpretations suffer from the fact that electron microscopy alone cannot identify the chemical nature of structures. I feel that further structural studies are needed to define the assembly state of these two proteins. To define a possible functional region in amelogenin, the effect of recombinantly prepared fragments of the protein has been tested by in vitro crystallization experiments.

A close example is the formation of biomineral-inspired, helical structures from chitin/calcium carbonate hybrids [4]. The authors felt inspired by the formation of the exoskeleton of lobster and crayfish. They observed a formation of liquid crystalline hybrids of natural chitin from waste products and calcium carbonate. An example of a remote relation with biomineralization is bioinspired thin film processing. Ceramic oxides are patterned on a self-assembled monolayer [5]. A related strategy is followed by using polymer brushes as the matrix, which bind microstructured calcite thin films [6, 7].

Little can be learned from the sequence of ameloblastin. Structural information is missing. The protein is cleaved by proteinase MMP20 during enamel formation. The intact protein has not been found in enamel, and the fragments are present in much smaller amounts than those of amelogenin. A surprisingly large and unique protein which is essential for enamel formation is enamelin [17]. It has been suggested that enamelin is involved with amelogenin expression. If enamelin is deleted, no enamel formation occurs, but the mechanism of its action is unclear (Fig.

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