Magnetite-binding proteins are in high demand for the functionalization of magnetic nanoparticles. Binding analysis of six previously uncharacterized proteins from the magnetotactic 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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Magnetite-binding proteins from the magnetotactic bacterium BW-1.
Nanoscale
December 2021
Max Planck Institute of Colloids and Interfaces, Mechano(bio)chemistry, Am Mühlenberg 1, 14476 Potsdam, Germany.
Magnetite-binding proteins are in high demand for the functionalization of magnetic nanoparticles. Binding analysis of six previously uncharacterized proteins from the magnetotactic 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.
View Article and Find Full Text PDFDecoding Biomineralization: Interaction of a Mad10-Derived Peptide with Magnetite Thin Films.
Nano Lett
November 2019
Department of Biomaterials , Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1 , 14476 Potsdam , Germany.
Protein-surface interactions play a pivotal role in processes as diverse as biomineralization, biofouling, and the cellular response to medical implants. In biomineralization processes, biomacromolecules control mineral deposition and architecture via complex and often unknown mechanisms. For studying these mechanisms, the formation of magnetite nanoparticles in magnetotactic bacteria has become an excellent model system.
View Article and Find Full Text PDFData on characterization of magnetic nanoparticles stabilized with fusion protein of Barstar and C-term part of Mms6.
Data Brief
December 2018
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya Street, Moscow 117997, Russia.
Mms6 is a protein that plays crucial role in the biomineralization and formation of magnetosomes in magnetotactic bacteria Magnetospirillum magneticum (strain AMB-1). We developed a fusion protein of C-term part of Mms6 and Barstar (natural inhibitor of ribonuclease Barnase), namely, Bs-C-Mms6. This protein successfully stabilized uncoated monocrystalline FeO magnetite nanoparticles in buffered solutions.
View Article and Find Full Text PDFSynthesis of Magnetic Nanoparticles Stabilized by Magnetite-Binding Protein for Targeted Delivery to Cancer Cells.
Dokl Biochem Biophys
July 2018
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
A new method for obtaining biomodified magnetite nanoparticles for targeted delivery to cells was developed. The method is based on the use of the C-terminal fragment of the Mms6 protein, which is involved in the magnetite biomineralization during the synthesis of magnetosomes in magnetotactic bacteria Magnetospirillum magneticum AMB-1, and the barnase*barstar high-affinity protein pair. The Mms6 protein fragment is required for stabilizing magnetite, and the barnase*barstar pair mediates the interaction between nanoparticles and the component for modification.
View Article and Find Full Text PDFMagnetite-Binding Flagellar Filaments Displaying the MamI Loop Motif.
Chembiochem
November 2016
Bio-Nanosystems Laboratory, Research Institute for Biomolecular and Chemical Engineering, University of Pannonia, Egyetem u. 10, 8200, Veszprém, Hungary.
This work aimed at developing a novel method for fabricating 1 D magnetite nanostructures with the help of mutated flagellar filaments. We constructed four different flagellin mutants displaying magnetite-binding motifs: two contained fragments of magnetosome-associated proteins from magnetotactic bacteria (MamI and Mms6), and synthetic sequences were used for the other two. A magnetic selection method identified the MamI mutant as having the highest binding affinity to magnetite.
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