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^*

^*Šī darba korespondējošais autors

Max Planck Institute of Colloids and Interfaces
Ben-Gurion University of the Negev
Aix-Marseille Université

Zinātniskās darbības rezultāts: Devums žurnālam › Zinātniskais raksts (žurnālā) › koleģiāli recenzēts

9 Atsauces (Scopus)

Kopsavilkums

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.

Oriģinālvaloda	Angļu
Lapas (no-līdz)	20396-20400
Lapu skaits	5
Žurnāls	Nanoscale
Sējums	13
Izdevuma numurs	48
DOIs	https://doi.org/10.1039/d1nr04870h
Publikācijas statuss	Publicēts - 28 dec. 2021
Ārēji publicēts	Jā

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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.\}",

note = "Publisher Copyright: {\textcopyright} 2021 The Royal Society of Chemistry.",

year = "2021",

month = dec,

day = "28",

doi = "10.1039/d1nr04870h",

language = "English",

volume = "13",

pages = "20396--20400",

journal = "Nanoscale",

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publisher = "Royal Society of Chemistry",

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TY - JOUR

T1 - Magnetite-binding proteins from the magnetotactic bacterium

T2 - Desulfamplus magnetovallimortis BW-1

AU - Pohl, Anna

AU - Young, Sarah A.E.

AU - Schmitz, Tara C.

AU - Farhadi, Daniel

AU - Zarivach, Raz

AU - Faivre, Damien

AU - Blank, Kerstin G.

PY - 2021/12/28

Y1 - 2021/12/28

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.

UR - https://www.scopus.com/pages/publications/85121695178

U2 - 10.1039/d1nr04870h

DO - 10.1039/d1nr04870h

M3 - Article

C2 - 34860229

AN - SCOPUS:85121695178

SN - 2040-3364

VL - 13

SP - 20396

EP - 20400

JO - Nanoscale

JF - Nanoscale

IS - 48

ER -

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

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