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Tuning properties of biomimetic magnetic nanoparticles by combining magnetosome associated proteins
The role of magnetosome associated proteins on the in vitro synthesis of magnetite nanoparticles has gained interest, both to obtain a better understanding of the magnetosome biomineralization process and to be able to produce novel magnetosome-like biomimetic nanoparticles. Up to now, only one reco...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6584501/ https://www.ncbi.nlm.nih.gov/pubmed/31217514 http://dx.doi.org/10.1038/s41598-019-45219-7 |
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author | Peigneux, Ana Jabalera, Ylenia Vivas, Ma Antonia Fernández Casares, Salvador Azuaga, Ana I. Jimenez-Lopez, Concepción |
author_facet | Peigneux, Ana Jabalera, Ylenia Vivas, Ma Antonia Fernández Casares, Salvador Azuaga, Ana I. Jimenez-Lopez, Concepción |
author_sort | Peigneux, Ana |
collection | PubMed |
description | The role of magnetosome associated proteins on the in vitro synthesis of magnetite nanoparticles has gained interest, both to obtain a better understanding of the magnetosome biomineralization process and to be able to produce novel magnetosome-like biomimetic nanoparticles. Up to now, only one recombinant protein has been used at the time to in vitro form biomimetic magnetite precipitates, being that a scenario far enough from what probably occurs in the magnetosome. In the present study, both Mms6 and MamC from Magnetococcus marinus MC-1 have been used to in vitro form biomimetic magnetites. Our results show that MamC and Mms6 have different, but complementary, effects on in vitro magnetite nucleation and growth. MamC seems to control the kinetics of magnetite nucleation while Mms6 seems to preferably control the kinetics for crystal growth. Our results from the present study also indicate that it is possible to combine both proteins to tune the properties of the resulting biomimetic magnetites. In particular, by changing the relative ratio of these proteins, better faceted and/or larger magnetite crystals with, consequently, different magnetic moment per particle could be obtained. This study provides with tools to obtain new biomimetic nanoparticles with a potential utility for biotechnological applications. |
format | Online Article Text |
id | pubmed-6584501 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-65845012019-06-26 Tuning properties of biomimetic magnetic nanoparticles by combining magnetosome associated proteins Peigneux, Ana Jabalera, Ylenia Vivas, Ma Antonia Fernández Casares, Salvador Azuaga, Ana I. Jimenez-Lopez, Concepción Sci Rep Article The role of magnetosome associated proteins on the in vitro synthesis of magnetite nanoparticles has gained interest, both to obtain a better understanding of the magnetosome biomineralization process and to be able to produce novel magnetosome-like biomimetic nanoparticles. Up to now, only one recombinant protein has been used at the time to in vitro form biomimetic magnetite precipitates, being that a scenario far enough from what probably occurs in the magnetosome. In the present study, both Mms6 and MamC from Magnetococcus marinus MC-1 have been used to in vitro form biomimetic magnetites. Our results show that MamC and Mms6 have different, but complementary, effects on in vitro magnetite nucleation and growth. MamC seems to control the kinetics of magnetite nucleation while Mms6 seems to preferably control the kinetics for crystal growth. Our results from the present study also indicate that it is possible to combine both proteins to tune the properties of the resulting biomimetic magnetites. In particular, by changing the relative ratio of these proteins, better faceted and/or larger magnetite crystals with, consequently, different magnetic moment per particle could be obtained. This study provides with tools to obtain new biomimetic nanoparticles with a potential utility for biotechnological applications. Nature Publishing Group UK 2019-06-19 /pmc/articles/PMC6584501/ /pubmed/31217514 http://dx.doi.org/10.1038/s41598-019-45219-7 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 Peigneux, Ana Jabalera, Ylenia Vivas, Ma Antonia Fernández Casares, Salvador Azuaga, Ana I. Jimenez-Lopez, Concepción Tuning properties of biomimetic magnetic nanoparticles by combining magnetosome associated proteins |
title | Tuning properties of biomimetic magnetic nanoparticles by combining magnetosome associated proteins |
title_full | Tuning properties of biomimetic magnetic nanoparticles by combining magnetosome associated proteins |
title_fullStr | Tuning properties of biomimetic magnetic nanoparticles by combining magnetosome associated proteins |
title_full_unstemmed | Tuning properties of biomimetic magnetic nanoparticles by combining magnetosome associated proteins |
title_short | Tuning properties of biomimetic magnetic nanoparticles by combining magnetosome associated proteins |
title_sort | tuning properties of biomimetic magnetic nanoparticles by combining magnetosome associated proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6584501/ https://www.ncbi.nlm.nih.gov/pubmed/31217514 http://dx.doi.org/10.1038/s41598-019-45219-7 |
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