Linear and orthogonal peptide templating of silicified protein fibres.
Org Biomol Chem
; 15(25): 5380-5385, 2017 Jun 27.
Article
em En
| MEDLINE
| ID: mdl-28620669
ABSTRACT
Biomineralisation is essential for biology. Specialist proteins use peptide motifs that catalyse mineral deposition into nano-to-microscale inorganic materials. Unlike in native proteins, the motifs incorporated into self-assembled fibres can persistently propagate on the microscopic scale enabling empirically defined silica nanostructures. Herein we show that the two main modes of motif templating - linear and orthogonal - in self-assembling, fibre-forming peptide sequences effectively silicify protein fibres. We show that the mere charge and morphology of protein fibres are not sufficient for silica deposition, but it is the synergy between fibrillogenesis and silica-specific motifs regularly spaced in fibres that ensures silica templating, regardless of the relative orientation of the motifs.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Proteínas
/
Dióxido de Silício
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article