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Linear and orthogonal peptide templating of silicified protein fibres

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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

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Publication details

The article was received on 09 May 2017, accepted on 08 Jun 2017 and first published on 09 Jun 2017


Article type: Paper
DOI: 10.1039/C7OB01134B
Citation: Org. Biomol. Chem., 2017, Advance Article
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    Linear and orthogonal peptide templating of silicified protein fibres

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

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