Data on characterization of magnetic nanoparticles stabilized with fusion protein of Barstar and C-term part of Mms6

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...

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Detalles Bibliográficos
Autores principales: Shipunova, Victoria O., Kotelnikova, Polina A., Aghayeva, Ulkar F., Stremovskiy, Oleg A., Schulga, Alexey A., Nikitin, Maxim P., Deyev, Sergey M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2018
Materias:
Materials Science
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6247411/
https://www.ncbi.nlm.nih.gov/pubmed/30505896
http://dx.doi.org/10.1016/j.dib.2018.10.173
Descripción
Sumario: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 Fe(3)O(4) magnetite nanoparticles in buffered solutions. Here, we present data regarding the synthesis and characterization of magnetite nanoparticles stabilized with Bs-C-Mms6. For further interpretation of the data presented in this article, please see the research article ‘Self-assembling nanoparticles biofunctionalized with magnetite-binding protein for the targeted delivery to HER2/neu overexpressing cancer cells’ (Shipunova et al., 2018) [1].

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