Biomagnetic nanoparticle formation and application

T. Matsunaga; H. Takeyama

doi:10.1016/S0968-5677(98)00037-6

Biomagnetic nanoparticle formation and application

T. Matsunaga^*, H. Takeyama

^*Corresponding author for this work

Research output: Contribution to journal › Conference article › peer-review

45 Citations (Scopus)

Abstract

Magnetospirillum sp. AMB-1 is a bacterium that synthesizes intracellular particles of magnetite (Fe₃O₄). A magA gene required for the synthesis of bacterial magnetic particles (BMPs) was isolated from this strain and its gene product (MagA protein) was characterized as an iron transport protein. Intracellular localization analysis of the MagA protein using magA-Luc fusion proteins showed that MagA protein is localized on the surface of the lipid bilayer covering the BMPs. One particular BMP-associated protein, designated MpsA, was also purified from this strain and characterized. By the fusion-protein method using mpsA-luc genes, it was demonstrated that Mps-protein is preferentially partitioned onto the BMP membrane. Furthermore, application of BMPs to immunoassay is also described.

Original language	English
Pages (from-to)	391-394
Number of pages	4
Journal	Supramolecular Science
Volume	5
Issue number	3-4
DOIs	https://doi.org/10.1016/S0968-5677(98)00037-6
Publication status	Published - 1998
Externally published	Yes
Event	Proceedings of the 11th Toyota Conference on Nanostructured Materials in Biological and Artificial Systems - Shizuoka, Jpn Duration: 1997 Nov 5 → 1997 Nov 8

ASJC Scopus subject areas

Engineering(all)

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10.1016/S0968-5677(98)00037-6

Cite this

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title = "Biomagnetic nanoparticle formation and application",

abstract = "Magnetospirillum sp. AMB-1 is a bacterium that synthesizes intracellular particles of magnetite (Fe3O4). A magA gene required for the synthesis of bacterial magnetic particles (BMPs) was isolated from this strain and its gene product (MagA protein) was characterized as an iron transport protein. Intracellular localization analysis of the MagA protein using magA-Luc fusion proteins showed that MagA protein is localized on the surface of the lipid bilayer covering the BMPs. One particular BMP-associated protein, designated MpsA, was also purified from this strain and characterized. By the fusion-protein method using mpsA-luc genes, it was demonstrated that Mps-protein is preferentially partitioned onto the BMP membrane. Furthermore, application of BMPs to immunoassay is also described.",

author = "T. Matsunaga and H. Takeyama",

year = "1998",

doi = "10.1016/S0968-5677(98)00037-6",

language = "English",

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pages = "391--394",

journal = "Supramolecular Science",

issn = "0968-5677",

publisher = "Elsevier BV",

number = "3-4",

note = "Proceedings of the 11th Toyota Conference on Nanostructured Materials in Biological and Artificial Systems ; Conference date: 05-11-1997 Through 08-11-1997",

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TY - JOUR

T1 - Biomagnetic nanoparticle formation and application

AU - Matsunaga, T.

AU - Takeyama, H.

PY - 1998

Y1 - 1998

N2 - Magnetospirillum sp. AMB-1 is a bacterium that synthesizes intracellular particles of magnetite (Fe3O4). A magA gene required for the synthesis of bacterial magnetic particles (BMPs) was isolated from this strain and its gene product (MagA protein) was characterized as an iron transport protein. Intracellular localization analysis of the MagA protein using magA-Luc fusion proteins showed that MagA protein is localized on the surface of the lipid bilayer covering the BMPs. One particular BMP-associated protein, designated MpsA, was also purified from this strain and characterized. By the fusion-protein method using mpsA-luc genes, it was demonstrated that Mps-protein is preferentially partitioned onto the BMP membrane. Furthermore, application of BMPs to immunoassay is also described.

AB - Magnetospirillum sp. AMB-1 is a bacterium that synthesizes intracellular particles of magnetite (Fe3O4). A magA gene required for the synthesis of bacterial magnetic particles (BMPs) was isolated from this strain and its gene product (MagA protein) was characterized as an iron transport protein. Intracellular localization analysis of the MagA protein using magA-Luc fusion proteins showed that MagA protein is localized on the surface of the lipid bilayer covering the BMPs. One particular BMP-associated protein, designated MpsA, was also purified from this strain and characterized. By the fusion-protein method using mpsA-luc genes, it was demonstrated that Mps-protein is preferentially partitioned onto the BMP membrane. Furthermore, application of BMPs to immunoassay is also described.

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DO - 10.1016/S0968-5677(98)00037-6

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SN - 0968-5677

VL - 5

SP - 391

EP - 394

JO - Supramolecular Science

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T2 - Proceedings of the 11th Toyota Conference on Nanostructured Materials in Biological and Artificial Systems

Y2 - 5 November 1997 through 8 November 1997

ER -

Biomagnetic nanoparticle formation and application

Abstract

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