title: Cryogenic transmission electron microscopy study of amelogenin self-assembly at different pH.
abstract: Cryogenic transmission electron microscopy (cryo-EM) was used to explore the self-assembly of recombinant murine amelogenin (rM179) in vitro. Our cryo-EM data showed that amelogenin self-assembly is a strongly pH-dependent process. At pH 4.4 the main fraction of the protein exists in a monomeric form, although some peculiar structures consisting of chains of monomers were also observed. At pH 5.8 large nanospheres comprising ring-like structures ~50 nm in diameter were the most abundant particle class. Similarly, at pH 8.0 amelogenins self-assembled into ring-like oligomers of different sizes, which subsequently assembled into nanospheres 15-20 nm in diameter. Furthermore, at pH 7.2, which is close to a physiological pH, branched chains of nanospheres were observed. Our results show that amelogenin assembly is a multistep hierarchical process and provides new insight into the control of enamel mineralization.
authors: Department of Oral Biology, Center for Craniofacial Regeneration, University of Pittsburgh, Pittsburgh, PA, USA.
authors: Ping-An
authors: PA
authors: Fang
authors: Henry C
authors: HC
authors: Margolis
authors: James F
authors: JF
authors: Conway
authors: James P
authors: JP
authors: Simmer
authors: Gary H
authors: GH
authors: Dickinson
authors: Elia
authors: E
authors: Beniash
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