Magnetite-binding proteins from the magnetotactic bacterium: Desulfamplus magnetovallimortis BW-1

Anna Pohl; Sarah A.E. Young; Tara C. Schmitz; Daniel Farhadi; Raz Zarivach; Damien Faivre; Kerstin G. Blank

doi:10.1039/d1nr04870h

Magnetite-binding proteins from the magnetotactic bacterium: Desulfamplus magnetovallimortis BW-1

Anna Pohl, Sarah A.E. Young, Tara C. Schmitz, Daniel Farhadi, Raz Zarivach, Damien Faivre, Kerstin G. Blank

Department of Life Sciences

Ben-Gurion University of the Negev

Research output: Contribution to journal › Article › peer-review

Abstract

Magnetite-binding proteins are in high demand for the functionalization of magnetic nanoparticles. Binding analysis of six previously uncharacterized proteins from the magnetotactic Deltaproteobacterium Desulfamplus magnetovallimortis BW-1 identified two new magnetite-binding proteins (Mad10, Mad11). These proteins can be utilized as affinity tags for the immobilization of recombinant fusion proteins to magnetite.

Original language	American English
Pages (from-to)	20396-20400
Number of pages	5
Journal	Nanoscale
Volume	13
Issue number	48
DOIs	https://doi.org/10.1039/d1nr04870h
State	Published - 28 Dec 2021

All Science Journal Classification (ASJC) codes

General Materials Science

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10.1039/d1nr04870h

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title = "Magnetite-binding proteins from the magnetotactic bacterium: Desulfamplus magnetovallimortis BW-1",

abstract = "Magnetite-binding proteins are in high demand for the functionalization of magnetic nanoparticles. Binding analysis of six previously uncharacterized proteins from the magnetotactic Deltaproteobacterium Desulfamplus magnetovallimortis BW-1 identified two new magnetite-binding proteins (Mad10, Mad11). These proteins can be utilized as affinity tags for the immobilization of recombinant fusion proteins to magnetite.",

author = "Anna Pohl and Young, {Sarah A.E.} and Schmitz, {Tara C.} and Daniel Farhadi and Raz Zarivach and Damien Faivre and Blank, {Kerstin G.}",

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AU - Farhadi, Daniel

AU - Zarivach, Raz

AU - Faivre, Damien

AU - Blank, Kerstin G.

PY - 2021/12/28

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N2 - Magnetite-binding proteins are in high demand for the functionalization of magnetic nanoparticles. Binding analysis of six previously uncharacterized proteins from the magnetotactic Deltaproteobacterium Desulfamplus magnetovallimortis BW-1 identified two new magnetite-binding proteins (Mad10, Mad11). These proteins can be utilized as affinity tags for the immobilization of recombinant fusion proteins to magnetite.

AB - Magnetite-binding proteins are in high demand for the functionalization of magnetic nanoparticles. Binding analysis of six previously uncharacterized proteins from the magnetotactic Deltaproteobacterium Desulfamplus magnetovallimortis BW-1 identified two new magnetite-binding proteins (Mad10, Mad11). These proteins can be utilized as affinity tags for the immobilization of recombinant fusion proteins to magnetite.

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U2 - 10.1039/d1nr04870h

DO - 10.1039/d1nr04870h

M3 - Article

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JO - Nanoscale

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ER -

Magnetite-binding proteins from the magnetotactic bacterium: Desulfamplus magnetovallimortis BW-1

Abstract

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