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Al-Garawi_et_al-2015-Angewandte_Chemie.pdf (2.52 MB)

Silica nanowires templated by amyloid-like fibrils

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posted on 2023-06-09, 07:28 authored by Zahraa S Al-Garawi, Julian R Thorpe, Louise SerpellLouise Serpell
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.

History

Publication status

  • Published

File Version

  • Published version

Journal

Angewandte Chemie

ISSN

0044-8249

Publisher

Wiley

Issue

45

Volume

127

Page range

13525-13529

Department affiliated with

  • Biochemistry Publications

Full text available

  • Yes

Peer reviewed?

  • Yes

Legacy Posted Date

2017-07-28

First Open Access (FOA) Date

2017-07-28

First Compliant Deposit (FCD) Date

2017-07-28

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