Magnetic Nanoclusters Coated with Albumin, Casein, and Gelatin: Size Tuning, Relaxivity, Stability, Protein Corona, and Application in Nuclear Magnetic Resonance Immunoassay
| Autor: | I. V. Byzov, Anatoly Ye. Yermakov, V. P. Timganova, P. V. Khramtsov, S. A. Zamorina, M. S. Bochkova, M. B. Rayev, Maria Kropaneva, Irina Barkina, Anton Nechaev |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
General Chemical Engineering
Nanoparticle PROTEIN Protein Corona Article Nanoclusters lcsh:Chemistry PROTEING COLLOIDAL STABILITY Blood serum antibody NANOPARTICLES streptavidin General Materials Science ASSAY Bovine serum albumin colloidal stability Bradford protein assay biology Chemistry Proteolytic enzymes assay protein G lcsh:QD1-999 Chemical engineering ANTIBODY STREPTAVIDIN biology.protein Magnetic nanoparticles nanoparticles protein |
| Zdroj: | Nanomaterials Nanomaterials, Vol 9, Iss 9, p 1345 (2019) Volume 9 Issue 9 |
| ISSN: | 2079-4991 |
| Popis: | The surface functionalization of magnetic nanoparticles improves their physicochemical properties and applicability in biomedicine. Natural polymers, including proteins, are prospective coatings capable of increasing the stability, biocompatibility, and transverse relaxivity (r2) of magnetic nanoparticles. In this work, we functionalized the nanoclusters of carbon-coated iron nanoparticles with four proteins: bovine serum albumin, casein, and gelatins A and B, and we conducted a comprehensive comparative study of their properties essential to applications in biosensing. First, we examined the influence of environmental parameters on the size of prepared nanoclusters and synthesized protein-coated nanoclusters with a tunable size. Second, we showed that protein coating does not significantly influence the r2 relaxivity of clustered nanoparticles however, the uniform distribution of individual nanoparticles inside the protein coating facilitates increased relaxivity. Third, we demonstrated the applicability of the obtained nanoclusters in biosensing by the development of a nuclear-magnetic-resonance-based immunoassay for the quantification of antibodies against tetanus toxoid. Fourth, the protein coronas of nanoclusters were studied using SDS-PAGE and Bradford protein assay. Finally, we compared the colloidal stability at various pH values and ionic strengths and in relevant complex media (i.e., blood serum, plasma, milk, juice, beer, and red wine), as well as the heat stability, resistance to proteolytic digestion, and shelf-life of protein-coated nanoclusters. |
| Databáze: | OpenAIRE |
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