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Artificial coiled coil biomineralisation protein for the synthesis of magnetic nanoparticles

Green synthesis of precise inorganic nanomaterials is a major challenge. Magnetotactic bacteria biomineralise magnetite nanoparticles (MNPs) within membrane vesicles (magnetosomes), which are embedded with dedicated proteins that control nanocrystal formation. Some such proteins are used in vitro to...

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Autores principales: Rawlings, Andrea E., Somner, Lori A., Fitzpatrick-Milton, Michaela, Roebuck, Thomas P., Gwyn, Christopher, Liravi, Panah, Seville, Victoria, Neal, Thomas J., Mykhaylyk, Oleksandr O., Baldwin, Stephen A., Staniland, Sarah S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6599041/
https://www.ncbi.nlm.nih.gov/pubmed/31253765
http://dx.doi.org/10.1038/s41467-019-10578-2
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author Rawlings, Andrea E.
Somner, Lori A.
Fitzpatrick-Milton, Michaela
Roebuck, Thomas P.
Gwyn, Christopher
Liravi, Panah
Seville, Victoria
Neal, Thomas J.
Mykhaylyk, Oleksandr O.
Baldwin, Stephen A.
Staniland, Sarah S.
author_facet Rawlings, Andrea E.
Somner, Lori A.
Fitzpatrick-Milton, Michaela
Roebuck, Thomas P.
Gwyn, Christopher
Liravi, Panah
Seville, Victoria
Neal, Thomas J.
Mykhaylyk, Oleksandr O.
Baldwin, Stephen A.
Staniland, Sarah S.
author_sort Rawlings, Andrea E.
collection PubMed
description Green synthesis of precise inorganic nanomaterials is a major challenge. Magnetotactic bacteria biomineralise magnetite nanoparticles (MNPs) within membrane vesicles (magnetosomes), which are embedded with dedicated proteins that control nanocrystal formation. Some such proteins are used in vitro to control MNP formation in green synthesis; however, these membrane proteins self-aggregate, making their production and use in vitro challenging and difficult to scale. Here, we provide an alternative solution by displaying active loops from biomineralisation proteins Mms13 and MmsF on stem-loop coiled-coil scaffold proteins (Mms13cc/MmsFcc). These artificial biomineralisation proteins form soluble, stable alpha-helical hairpin monomers, and MmsFcc successfully controls the formation of MNP when added to magnetite synthesis, regulating synthesis comparably to native MmsF. This study demonstrates how displaying active loops from membrane proteins on coiled-coil scaffolds removes membrane protein solubility issues, while retains activity, enabling a generic approach to readily-expressible, versatile, artificial membrane proteins for more accessible study and exploitation.
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spelling pubmed-65990412019-07-01 Artificial coiled coil biomineralisation protein for the synthesis of magnetic nanoparticles Rawlings, Andrea E. Somner, Lori A. Fitzpatrick-Milton, Michaela Roebuck, Thomas P. Gwyn, Christopher Liravi, Panah Seville, Victoria Neal, Thomas J. Mykhaylyk, Oleksandr O. Baldwin, Stephen A. Staniland, Sarah S. Nat Commun Article Green synthesis of precise inorganic nanomaterials is a major challenge. Magnetotactic bacteria biomineralise magnetite nanoparticles (MNPs) within membrane vesicles (magnetosomes), which are embedded with dedicated proteins that control nanocrystal formation. Some such proteins are used in vitro to control MNP formation in green synthesis; however, these membrane proteins self-aggregate, making their production and use in vitro challenging and difficult to scale. Here, we provide an alternative solution by displaying active loops from biomineralisation proteins Mms13 and MmsF on stem-loop coiled-coil scaffold proteins (Mms13cc/MmsFcc). These artificial biomineralisation proteins form soluble, stable alpha-helical hairpin monomers, and MmsFcc successfully controls the formation of MNP when added to magnetite synthesis, regulating synthesis comparably to native MmsF. This study demonstrates how displaying active loops from membrane proteins on coiled-coil scaffolds removes membrane protein solubility issues, while retains activity, enabling a generic approach to readily-expressible, versatile, artificial membrane proteins for more accessible study and exploitation. Nature Publishing Group UK 2019-06-28 /pmc/articles/PMC6599041/ /pubmed/31253765 http://dx.doi.org/10.1038/s41467-019-10578-2 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Rawlings, Andrea E.
Somner, Lori A.
Fitzpatrick-Milton, Michaela
Roebuck, Thomas P.
Gwyn, Christopher
Liravi, Panah
Seville, Victoria
Neal, Thomas J.
Mykhaylyk, Oleksandr O.
Baldwin, Stephen A.
Staniland, Sarah S.
Artificial coiled coil biomineralisation protein for the synthesis of magnetic nanoparticles
title Artificial coiled coil biomineralisation protein for the synthesis of magnetic nanoparticles
title_full Artificial coiled coil biomineralisation protein for the synthesis of magnetic nanoparticles
title_fullStr Artificial coiled coil biomineralisation protein for the synthesis of magnetic nanoparticles
title_full_unstemmed Artificial coiled coil biomineralisation protein for the synthesis of magnetic nanoparticles
title_short Artificial coiled coil biomineralisation protein for the synthesis of magnetic nanoparticles
title_sort artificial coiled coil biomineralisation protein for the synthesis of magnetic nanoparticles
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6599041/
https://www.ncbi.nlm.nih.gov/pubmed/31253765
http://dx.doi.org/10.1038/s41467-019-10578-2
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