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- W3011291335 abstract "Magnetic nanoparticles (MNPs) chelating with metal ions can specifically interact with poly-histidine peptides and facilitate immobilization and purification of proteins with poly-histidine tags. Fabrication of MNPs is generally complicated and time consuming. In this paper, we report the preparation of Ni(ii) ion chelated MNPs (Ni-MNPs) in two stages for protein immobilization and purification. In the first stage, organic ligands including pentadentate tris (carboxymethyl) ethylenediamine (TED) and tridentate iminodiacetic acid (IDA) and inorganic Fe3O4-SiO2 MNPs were synthesized separately. In the next stage, ligands were grafted to the surface of MNPs and MNPs with a TED or IDA modified surface were acquired, followed by chelating with Ni(ii) ions. The Ni(ii) ion chelated forms of MNPs (Ni-MNPs) were characterized including morphology, surface charge, structure, size distribution and magnetic response. Taking a his-tagged glycoside hydrolase DspB (Dispersin B) as the protein representative, specific interactions were confirmed between DspB and Ni-MNPs. Purification of his-tagged DspB was achieved with Ni-MNPs that exhibited better performance in terms of purity and activity of DspB than commercial Ni-NTA. Ni-MNPs as enzyme carriers for DspB also exhibited good compatibility and reasonable reusability as well as improved performance in various conditions." @default.
- W3011291335 created "2020-03-23" @default.
- W3011291335 creator A5012073852 @default.
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- W3011291335 creator A5068108543 @default.
- W3011291335 creator A5072823996 @default.
- W3011291335 date "2020-01-01" @default.
- W3011291335 modified "2023-10-17" @default.
- W3011291335 title "Synthesis of magnetic nanoparticles with an IDA or TED modified surface for purification and immobilization of poly-histidine tagged proteins" @default.
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- W3011291335 doi "https://doi.org/10.1039/c9ra10473a" @default.
- W3011291335 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35495316" @default.
- W3011291335 hasPublicationYear "2020" @default.
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