Designed Self-Assembled β-Sheet Peptide Fibrils as Templates for Silica Nanotubes

Sol–gel condensation of tetraethoxysilane in the presence of designed self‐assembled β‐sheet peptide fibril templates, followed by template extraction, yields hollow silica nanotubes. The nanotubes are hundreds of nanometers long and possess a central pore of ∼ 3.5 nm, determined by the fibril templ...

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Published inAdvanced functional materials Vol. 14; no. 1; pp. 31 - 37
Main Authors Meegan, J. E., Aggeli, A., Boden, N., Brydson, R., Brown, A. P., Carrick, L., Brough, A. R., Hussain, A., Ansell, R. J.
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 01.01.2004
WILEY‐VCH Verlag
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Summary:Sol–gel condensation of tetraethoxysilane in the presence of designed self‐assembled β‐sheet peptide fibril templates, followed by template extraction, yields hollow silica nanotubes. The nanotubes are hundreds of nanometers long and possess a central pore of ∼ 3.5 nm, determined by the fibril template diameter. The effects of synthesis conditions have been investigated and the resultant silica materials characterized by various techniques. Silica nanostructures with various morphologies have been produced previously using supramolecular organic assemblies as templates. Hollow nano‐ or microtubes, which may have applications in separations, catalysis, nano‐optics, and ‐electronics have been of particular interest. Peptide‐based templates are especially interesting because of their relevance to biological silica microstructure formation. The new fibrillar peptide templates described here have the advantages of prescribed diameter, twist pitch, and handedness, which should impart chirality on the resulting silica nanotubes, providing control of the internal surface architecture by appropriate peptide design. Self‐assembling peptides provide a versatile template system for the production of inorganic nanotubes by controlled sol–gel deposition. Well‐defined hollow silica nanotubes (see Figure) have been prepared consisting of 89 % Q4‐type silica and of ∼ 20 nm outside diameter with ∼ 3.5 nm diameter central pores using a designed positively charged L‐P‐3 peptide fibril template.
Bibliography:istex:932D378774606AE25357F87788F5D283F77C682B
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We are grateful to the following co-workers at the University of Leeds: Howard Daniels for assistance with TEM, Adrian Hick (Department of Biology) and Dr. Jeff Keen (Department of Biochemistry and Molecular Biology) for providing access to TEM and HPLC facilities. We also thank Dr. Irena Nyrkova (University of Moscow, Department of Physics) for the schematic picture of a fibril. AA gratefully acknowledges the support of the Royal Society through a University Research Fellowship. ARB is grateful to the University of Leeds for a University Research Fellowship.
ArticleID:ADFM200304477
We are grateful to the following co‐workers at the University of Leeds: Howard Daniels for assistance with TEM, Adrian Hick (Department of Biology) and Dr. Jeff Keen (Department of Biochemistry and Molecular Biology) for providing access to TEM and HPLC facilities. We also thank Dr. Irena Nyrkova (University of Moscow, Department of Physics) for the schematic picture of a fibril. AA gratefully acknowledges the support of the Royal Society through a University Research Fellowship. ARB is grateful to the University of Leeds for a University Research Fellowship.
ISSN:1616-301X
1616-3028
DOI:10.1002/adfm.200304477