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Journal Article

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

MPS-Authors
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Pohl,  Anna
Damien Faivre, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Young,  Sarah
Amaia Cipitria, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

Schmitz,  Tara C.
Kerstin Blank, Mechano(bio)chemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons243650

Farhadi,  Daniel
Kerstin Blank, Mechano(bio)chemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Faivre,  Damien
Damien Faivre, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons134416

Blank,  Kerstin G.
Kerstin Blank, Mechano(bio)chemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Citation

Pohl, A., Young, S., Schmitz, T. C., Farhadi, D., Zarivach, R., Faivre, D., et al. (2021). Magnetite-binding proteins from the magnetotactic bacterium Desulfamplus magnetovallimortis BW-1. Nanoscale, 13(48), 20396-20400. doi:10.1039/D1NR04870H.


Cite as: https://hdl.handle.net/21.11116/0000-0009-96AD-B
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.