Co-assemblies of polyoxometalate {Mo72Fe30}/double-tailed magnetic-surfactant for magnetic-driven anchorage and enrichment of protein
Autor: | Wenrong Zhao, Jiwei Cui, J. David Van Horn, Jingcheng Hao |
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Rok vydání: | 2019 |
Předmět: |
Aqueous solution
Chemistry 02 engineering and technology 010402 general chemistry 021001 nanoscience & nanotechnology 01 natural sciences 0104 chemical sciences Surfaces Coatings and Films Electronic Optical and Magnetic Materials Biomaterials Magnetization chemistry.chemical_compound Colloid and Surface Chemistry Pulmonary surfactant Chemical engineering Myoglobin Covalent bond Amphiphile Polyoxometalate Molecule 0210 nano-technology |
Zdroj: | Journal of Colloid and Interface Science. 536:88-97 |
ISSN: | 0021-9797 |
Popis: | Covalent grafting and electrostatic-driven assembly have been two strategies in constructing well-defined polyoxometalate (POM) assemblies to produce specific morphologies and desirable properties. The modification of anionic counter-ions of amphiphilic compounds in POM-surfactant hybrid systems is still unexploited. Herein, we report the co-assembly of a synthetic double-tailed magnetic surfactant (MagSurf), (C18)2C2N+[FeCl4]−, and POM, {Mo72Fe30}. The magnetic aggregate (POM/MagSurf) results from the building up hierarchical structures at a time-dependent interface. In this construct, both the MagSurfs and {Mo72Fe30} POMs contribute to and mutually strengthen the magnetization of the designed magnetic assembles. Interestingly, the POM/MagSurf aggregates are compatible with aqueous mixtures and successfully employed to serve as magnetic transporting vehicles to anchor and deliver a protein molecule, myoglobin (Mb). Upon applying a magnetic field (0.3 T), the magnetic aggregates induced a directional migration and enrichment of the Mb protein (71–90%). During this process, the protein/POM/MagSurf complexes exhibited strong interactions facilitating stable anchoring and efficient enrichment of the Mb. |
Databáze: | OpenAIRE |
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