Silica nanowires templated by amyloid-like fibrils

Al-Garawi, Zahraa S, Thorpe, Julian R and Serpell, Louise C (2015) Silica nanowires templated by amyloid-like fibrils. Angewandte Chemie, 127 (45). pp. 13525-13529. ISSN 0044-8249 (Accepted)

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Abstract

Many peptides self-assemble to form amyloid fibrils. We previously explored the sequence propensity to form amyloid using variants of a designed peptide with sequence KFFEAAAKKFFE. These variant peptides form highly stable amyloid fibrils with varied lateral assembly and are ideal to template further assembly of non-proteinaceous material. Herein, we show that the fibrils formed by peptide variants can be coated with a layer of silica to produce silica nanowires using tetraethyl-orthosilicate. The resulting nanowires were characterized using electron microscopy (TEM), X-ray fiber diffraction, FTIR and cross-section EM to reveal a nanostructure with peptidic core. Lysine residues play a role in templating the formation of silica on the fibril surface and, using this library of peptides, we have explored the contributions of lysine as well as arginine to silica templating, and find that sequence plays an important role in determining the physical nature and structure of the resulting nanowires.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science > QD Chemistry
Depositing User: Louise Serpell
Date Deposited: 28 Jul 2017 10:51
Last Modified: 28 Jul 2017 11:02
URI: http://sro.sussex.ac.uk/id/eprint/69506

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