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      Chemically and thermally stable silica nanowires with a β-sheet peptide core for bionanotechnology

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          Abstract

          Background

          A series of amyloidogenic peptides based on the sequence KFFEAAAKKFFE template the silica precursor, tetraethyl orthosilicate to form silica-nanowires containing a cross-β peptide core.

          Results

          Investigation of the stability of these fibres reveals that the silica layers protect the silica-nanowires allowing them to maintain their shape and physical and chemical properties after incubation with organic solvents such as 2-propanol, ethanol, and acetonitrile, as well as in a strong acidic solution at pH 1.5. Furthermore, these nanowires were thermally stable in an aqueous solution when heated up to 70 °C, and upon autoclaving. They also preserved their conformation following incubation up to 4 weeks under these harsh conditions, and showed exceptionally high physical stability up to 1000 °C after ageing for 12 months. We show that they maintain their β-sheet peptide core even after harsh treatment by confirming the β-sheet content using Fourier transform infrared spectra. The silica nanowires show significantly higher chemical and thermal stability compared to the unsiliconised fibrils.

          Conclusions

          The notable chemical and thermal stability of these silica nanowires points to their potential for use in microelectromechanics processes or fabrication for nanotechnological devices.

          Electronic supplementary material

          The online version of this article (doi:10.1186/s12951-016-0231-8) contains supplementary material, which is available to authorized users.

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          Most cited references25

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          One-Dimensional Nanostructures: Synthesis, Characterization, and Applications

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            Fourier transform infrared spectroscopic analysis of protein secondary structures.

            Infrared spectroscopy is one of the oldest and well established experimental techniques for the analysis of secondary structure of polypeptides and proteins. It is convenient, non-destructive, requires less sample preparation, and can be used under a wide variety of conditions. This review introduces the recent developments in Fourier transform infrared (FTIR) spectroscopy technique and its applications to protein structural studies. The experimental skills, data analysis, and correlations between the FTIR spectroscopic bands and protein secondary structure components are discussed. The applications of FTIR to the secondary structure analysis, conformational changes, structural dynamics and stability studies of proteins are also discussed.
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              Silica-based mesoporous organic-inorganic hybrid materials.

              Mesoporous organic-inorganic hybrid materials, a new class of materials characterized by large specific surface areas and pore sizes between 2 and 15 nm, have been obtained through the coupling of inorganic and organic components by template synthesis. The incorporation of functionalities can be achieved in three ways: by subsequent attachment of organic components onto a pure silica matrix (grafting), by simultaneous reaction of condensable inorganic silica species and silylated organic compounds (co-condensation, one-pot synthesis), and by the use of bissilylated organic precursors that lead to periodic mesoporous organosilicas (PMOs). This Review gives an overview of the preparation, properties, and potential applications of these materials in the areas of catalysis, sorption, chromatography, and the construction of systems for controlled release of active compounds, as well as molecular switches, with the main focus being on PMOs.
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                Author and article information

                Contributors
                zm58@sussex.ac.uk
                G.Kostakis@sussex.ac.uk
                L.C.Serpell@sussex.ac.uk
                Journal
                J Nanobiotechnology
                J Nanobiotechnology
                Journal of Nanobiotechnology
                BioMed Central (London )
                1477-3155
                1 December 2016
                1 December 2016
                2016
                : 14
                Affiliations
                [1 ]School of Life Sciences, University of Sussex, East Sussex, Falmer, BN1 9QG UK
                [2 ]Chemistry Department, College of Sciences, Al-Mustansyria University, Baghdad, Iraq
                Article
                231
                10.1186/s12951-016-0231-8
                5134108
                27905946
                8607b4d8-2e5b-4b90-99a9-70b5ca9a7c84
                © The Author(s) 2016

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

                Funding
                Funded by: FundRef http://dx.doi.org/10.13039/501100000268, Biotechnology and Biological Sciences Research Council;
                Award ID: BB/E009042/1
                Award Recipient :
                Categories
                Research
                Custom metadata
                © The Author(s) 2016

                Biotechnology
                amyloid fibril,chemical stability,thermal stability,nanostructures,ftir,ultra microtome,tga analysis

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