Linear and orthogonal peptide templating of silicified protein fibres

Angelo Bella, Santanu Ray, Maxim G. Ryadnov

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)5380-5385
Number of pages6
JournalOrganic and Biomolecular Chemistry
Volume15
Issue number25
DOIs
Publication statusPublished - 9 Jun 2017

Fingerprint Dive into the research topics of 'Linear and orthogonal peptide templating of silicified protein fibres'. Together they form a unique fingerprint.

  • Equipment

  • Cite this