Issue 25, 2017

Linear and orthogonal peptide templating of silicified protein fibres

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.

Graphical abstract: Linear and orthogonal peptide templating of silicified protein fibres

Supplementary files

Article information

Article type
Paper
Submitted
09 may. 2017
Accepted
08 jun. 2017
First published
09 jun. 2017

Org. Biomol. Chem., 2017,15, 5380-5385

Linear and orthogonal peptide templating of silicified protein fibres

A. Bella, S. Ray and M. G. Ryadnov, Org. Biomol. Chem., 2017, 15, 5380 DOI: 10.1039/C7OB01134B

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