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Enzymatic Synthesis of Magnetic Nanoparticles

We report the first in vitro enzymatic synthesis of paramagnetic and antiferromagnetic nanoparticles toward magnetic ELISA reporting. With our procedure, alkaline phosphatase catalyzes the dephosphorylation of l-ascorbic-2-phosphate, which then serves as a reducing agent for salts of iron, gadoliniu...

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Autores principales: Kolhatkar, Arati G., Dannongoda, Chamath, Kourentzi, Katerina, Jamison, Andrew C., Nekrashevich, Ivan, Kar, Archana, Cacao, Eliedonna, Strych, Ulrich, Rusakova, Irene, Martirosyan, Karen S., Litvinov, Dmitri, Lee, T. Randall, Willson, Richard C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4425032/
https://www.ncbi.nlm.nih.gov/pubmed/25854425
http://dx.doi.org/10.3390/ijms16047535
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author Kolhatkar, Arati G.
Dannongoda, Chamath
Kourentzi, Katerina
Jamison, Andrew C.
Nekrashevich, Ivan
Kar, Archana
Cacao, Eliedonna
Strych, Ulrich
Rusakova, Irene
Martirosyan, Karen S.
Litvinov, Dmitri
Lee, T. Randall
Willson, Richard C.
author_facet Kolhatkar, Arati G.
Dannongoda, Chamath
Kourentzi, Katerina
Jamison, Andrew C.
Nekrashevich, Ivan
Kar, Archana
Cacao, Eliedonna
Strych, Ulrich
Rusakova, Irene
Martirosyan, Karen S.
Litvinov, Dmitri
Lee, T. Randall
Willson, Richard C.
author_sort Kolhatkar, Arati G.
collection PubMed
description We report the first in vitro enzymatic synthesis of paramagnetic and antiferromagnetic nanoparticles toward magnetic ELISA reporting. With our procedure, alkaline phosphatase catalyzes the dephosphorylation of l-ascorbic-2-phosphate, which then serves as a reducing agent for salts of iron, gadolinium, and holmium, forming magnetic precipitates of Fe(45±14)Gd(5±2)O(50±15) and Fe(42±4)Ho(6±4)O(52±5). The nanoparticles were found to be paramagnetic at 300 K and antiferromagnetic under 25 K. Although weakly magnetic at 300 K, the room-temperature magnetization of the nanoparticles found here is considerably greater than that of analogous chemically-synthesized Ln(x)Fe(y)O(z) (Ln = Gd, Ho) samples reported previously. At 5 K, the nanoparticles showed a significantly higher saturation magnetization of 45 and 30 emu/g for Fe(45±14)Gd(5±2)O(50±15) and Fe(42±4)Ho(6±4)O(52±5), respectively. Our approach of enzymatically synthesizing magnetic labels reduces the cost and avoids diffusional mass-transfer limitations associated with pre-synthesized magnetic reporter particles, while retaining the advantages of magnetic sensing.
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spelling pubmed-44250322015-05-20 Enzymatic Synthesis of Magnetic Nanoparticles Kolhatkar, Arati G. Dannongoda, Chamath Kourentzi, Katerina Jamison, Andrew C. Nekrashevich, Ivan Kar, Archana Cacao, Eliedonna Strych, Ulrich Rusakova, Irene Martirosyan, Karen S. Litvinov, Dmitri Lee, T. Randall Willson, Richard C. Int J Mol Sci Article We report the first in vitro enzymatic synthesis of paramagnetic and antiferromagnetic nanoparticles toward magnetic ELISA reporting. With our procedure, alkaline phosphatase catalyzes the dephosphorylation of l-ascorbic-2-phosphate, which then serves as a reducing agent for salts of iron, gadolinium, and holmium, forming magnetic precipitates of Fe(45±14)Gd(5±2)O(50±15) and Fe(42±4)Ho(6±4)O(52±5). The nanoparticles were found to be paramagnetic at 300 K and antiferromagnetic under 25 K. Although weakly magnetic at 300 K, the room-temperature magnetization of the nanoparticles found here is considerably greater than that of analogous chemically-synthesized Ln(x)Fe(y)O(z) (Ln = Gd, Ho) samples reported previously. At 5 K, the nanoparticles showed a significantly higher saturation magnetization of 45 and 30 emu/g for Fe(45±14)Gd(5±2)O(50±15) and Fe(42±4)Ho(6±4)O(52±5), respectively. Our approach of enzymatically synthesizing magnetic labels reduces the cost and avoids diffusional mass-transfer limitations associated with pre-synthesized magnetic reporter particles, while retaining the advantages of magnetic sensing. MDPI 2015-04-03 /pmc/articles/PMC4425032/ /pubmed/25854425 http://dx.doi.org/10.3390/ijms16047535 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Kolhatkar, Arati G.
Dannongoda, Chamath
Kourentzi, Katerina
Jamison, Andrew C.
Nekrashevich, Ivan
Kar, Archana
Cacao, Eliedonna
Strych, Ulrich
Rusakova, Irene
Martirosyan, Karen S.
Litvinov, Dmitri
Lee, T. Randall
Willson, Richard C.
Enzymatic Synthesis of Magnetic Nanoparticles
title Enzymatic Synthesis of Magnetic Nanoparticles
title_full Enzymatic Synthesis of Magnetic Nanoparticles
title_fullStr Enzymatic Synthesis of Magnetic Nanoparticles
title_full_unstemmed Enzymatic Synthesis of Magnetic Nanoparticles
title_short Enzymatic Synthesis of Magnetic Nanoparticles
title_sort enzymatic synthesis of magnetic nanoparticles
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4425032/
https://www.ncbi.nlm.nih.gov/pubmed/25854425
http://dx.doi.org/10.3390/ijms16047535
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