Matching 4.7-Å XRD spacing in amelogenin nanoribbons and enamel matrix.
J Dent Res
; 93(9): 918-22, 2014 Sep.
Article
em En
| MEDLINE
| ID: mdl-25048248
ABSTRACT
The recent discovery of conditions that induce nanoribbon structures of amelogenin protein in vitro raises questions about their role in enamel formation. Nanoribbons of recombinant human full-length amelogenin (rH174) are about 17 nm wide and self-align into parallel bundles; thus, they could act as templates for crystallization of nanofibrous apatite comprising dental enamel. Here we analyzed the secondary structures of nanoribbon amelogenin by x-ray diffraction (XRD) and Fourier transform infrared spectroscopy (FTIR) and tested if the structural motif matches previous data on the organic matrix of enamel. XRD analysis showed that a peak corresponding to 4.7 Å is present in nanoribbons of amelogenin. In addition, FTIR analysis showed that amelogenin in the form of nanoribbons was comprised of ß-sheets by up to 75%, while amelogenin nanospheres had predominantly random-coil structure. The observation of a 4.7-Å XRD spacing confirms the presence of ß-sheets and illustrates structural parallels between the in vitro assemblies and structural motifs in developing enamel.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Esmalte Dentário
/
Amelogenina
/
Nanopartículas
Limite:
Humans
Idioma:
En
Revista:
J Dent Res
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
Estados Unidos