Shipunova Victoria O, Kotelnikova Polina A, Aghayeva Ulkar F, Stremovskiy Oleg A, Schulga Alexey A, Nikitin Maxim P, Deyev Sergey M
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya Street, Moscow 117997, Russia.
National Research Nuclear University MEPhI, Kashirskoe shosse 31, Moscow 115409, Russia.
Data Brief. 2018 Nov 3;21:1659-1663. doi: 10.1016/j.dib.2018.10.173. eCollection 2018 Dec.
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. 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].
Mms6是一种在趋磁细菌磁螺菌（菌株AMB-1）中对磁小体的生物矿化和形成起关键作用的蛋白质。我们开发了一种Mms6 C端部分与Barstar（核糖核酸酶Barnase的天然抑制剂）的融合蛋白，即Bs-C-Mms6。该蛋白成功地在缓冲溶液中稳定了未包覆的单晶FeO磁铁矿纳米颗粒。在此，我们展示了关于用Bs-C-Mms6稳定的磁铁矿纳米颗粒的合成和表征的数据。为进一步解释本文所呈现的数据，请参阅研究文章《用磁铁矿结合蛋白生物功能化的自组装纳米颗粒靶向递送至HER2/neu过表达癌细胞》（Shipunova等人，2018年）[1]。
