Cryogenic transmission electron microscopy study of amelogenin self-assembly at different pH.
Cells Tissues Organs
; 194(2-4): 166-70, 2011.
Article
em En
| MEDLINE
| ID: mdl-21597263
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Microscopia Crioeletrônica
/
Microscopia Eletrônica de Transmissão
/
Amelogenina
Limite:
Animals
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article