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 in | Advanced functional materials Vol. 14; no. 1; pp. 31 - 37 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Weinheim
WILEY-VCH Verlag
01.01.2004
WILEY‐VCH Verlag |
Subjects | |
Online Access | Get full text |
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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. |
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Bibliography: | istex:932D378774606AE25357F87788F5D283F77C682B ark:/67375/WNG-FJHGX7H4-W 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 |