Direct Immobilization of Coagulation Factor VIII on Au/Fe3O4 Shell/Core Magnetic Nanoparticles for Analytical Application
Trends in Peptide and Protein Sciences,
Vol. 1 No. 1 (2016),
4 October 2016
,
Page 20-26
https://doi.org/10.22037/tpps.v1i1.13301
Abstract
Protein-coated nanoparticles have diverse applications in biomedical science. The protein hydrophobic domains or surface electrostatic charge conducts adsorption of proteins to different surfaces. This property can be customized to immobilize specific molecules on solid supports for experimental screenings or purification processes. To develop highly selective affinity ligands—such as aptamers—against specific protein targets, protein-coated magnetic particles have been successfully applied. This approach could be highly efficient in affinity ligand development against coagulation factor VIII.In this study, magnetic nanoparticles were prepared by co-precipitation method and, then, a gold coating was run on the MNPs’ surface. The gold coating could add some attractive specifications to the protein immobilized nanoparticles during the aptamer selection process, such as simultaneous affinity determination of aptameric oligonucleotides by fluorescence-based methods. The gold surface has been indicated as a specific feature for covalent binding to the sulphur functional groups of various molecules. In proteins, sulphur units of cysteine or methionine might be bound covalently to the gold surface. In addition, nonspecific and non-covalent attachment of proteins to the gold particles may be performed. Therefore, a series of samples containing different mass ratios of protein to gold magnetic nanoparticles (GMNPs) were evaluated to find the best conditions for coagulation factor VIII immobilization. The results showed that the best condition for high coating efficiency was 48 h incubation at 4 ºC of protein and GMNPs with a mass ratio of 0.5% in PBS 25mM, with pH=7 as binding buffer.
Highlights:
- Magnetic nanoparticles are the most attractive nanostructures in biomedical and bio-analytical fields.
- The protein coating on MNPs has been found to have wide clinical and analytical applications.
- Coagulation factor VIII (FVIII) is a valuable therapeutic human protein in the market.
- Attachment of a large protein like F VIII to GMNPs is affected by various environmental factors.
- Gold magnetic nanoparticles
- Human coagulation factor VIII
- Protein immobilization
- Surface coating
How to Cite
References
Ayyar, B. V., Arora, S., Murphy, C. and R. O’Kennedy, (2012)."Affinity chromatography as a tool for antibody purification."Methods, 56(2):116-129.
Bao, F., Yao, J. L. and R. A. Gu, (2009). "Synthesis of magnetic Fe2O3/Au core/shell nanoparticles for bioseparation and immunoassay based on surface-enhanced Raman spectroscopy." Langmuir, 25(18): 10782-10787.
Burnouf, T. (2007). "Modern plasma fractionation." Transfusion Medicine Reviews, 21(2): 101-117.
Burnouf, T. and M. Radosevich, (2001). "Affinity chromatography in the industrial purification of plasma proteins for therapeutic use." Journal of Biochemical and Biophysical Methods, 49(1): 575-586.
Chatterjee, K., Sarkar, S., Rao, K. J. and S. Paria, (2014). "Core/shell nanoparticles in biomedical applications." Advances in Colloid and Interface Science, 209: 8-39.
Colombo, M., Carregal-Romero, S., Casula, M. F., Gutierrez, L., Morales, M. P., Boehm, I. B., Heverhagen, J. T., Prosperi, D. and W. J. Parak, (2012). "Biological applications of magnetic nanoparticles." Chemical Society Reviews, 41(11): 4306-4334.
Esmaeilpour, M., Javidi, J. and M. Zandi, (2014). "Preparation and characterization of Fe3O4@ SiO2@ PMA: AS an efficient and recyclable nanocatalyst for the synthesis of 1-amidoalkyl-2- naphthols." Materials Research Bulletin, 55: 78-87.
Gouw, S. C., van der Bom, J. G., Ljung, R., Escuriola, C., Cid, A. R., Claeyssens-Donadel, S., van Geet, C., Kenet, G., Mäkipernaa, A., Molinari, A. C. and W. Muntean, (2013). "Factor VIII products and inhibitor development in severe hemophilia A." New England Journal of Medicine, 368(3): 231-239.
Hage, D. S., Anguizola, J. A., Bi, C., Li, R., Matsuda, R., Papastavros, E., Pfaunmiller, E., Vargas, J. and X. Zheng, (2012). "Pharmaceutical and biomedical applications of affinity chromatography: recent trends and developments." Journal of Pharmaceutical and Biomedical Analysis, 69: 93-105.
Indira, T. and P. Lakshmi, (2010). "Magnetic nanoparticles—a review." International Journal of Pharmaceutical Sciences and Nanotechnology,3(3):1035-1042.
Kaufman, E. D., Belyea, J., Johnson, M. C., Nicholson, Z. M., Ricks, J. L., Shah, P. K., Bayless, M., Pettersson, T., Feldotö, Z., Blomberg, E. and P. Claesson, (2007). "Probing protein adsorption onto mercaptoundecanoic acid stabilized gold nanoparticles and surfaces by quartz crystal microbalance and ζ-potential measurements." Langmuir, 23(11): 6053-6062.
Kruger, N. J. (2009). "The Bradford method for protein quantitation." In: The Protein Protocols Handbook, walker J. M. (ed), Springer, Singapore, 17-24.
Lim, H. K., Kim, I.-H., Nam, H. Y., Shin, S. and S. S. Hah, (2013). "Aptamer-Based Alternatives to the Conventional Immobilized Metal Affinity Chromatography for Purification of His-Tagged Proteins." Analytical Letters, 46(3): 407-415. doi: 10.1080/00032719.2012.721105
Lönne, M., Bolten, S., Lavrentieva, A., Stahl, F., Scheper, T. and J. G. Walter, (2015). "Development of an aptamer-based affinity purification method for vascular endothelial growth factor." Biotechnology Reports, 8: 16-23. doi: 10.1016/j.btre.2015.08.006
Qiao, L., Lv, B., Feng, X. and C. Li, (2015). "A new application of aptamer: One-step purification and immobilization of enzyme from cell lysates for biocatalysis." Journal of Biotechnology, 203: 68-76. doi: 10.1016/j.jbiotec.2015.03.014
Qiu, J. D., Peng, H. P., Liang, R. P. and X. H. Xia, (2010). "Facile preparation of magnetic core–shell Fe3O4@ Au nanoparticle/ myoglobin biofilm for direct electrochemistry." Biosensors and Bioelectronics, 25(6): 1447-1453.
Rodrigues, E. S., Verinaud, C. I., Oliveira, D. S., Raw, I., Lopes, A. P., Martins, E. A. and E. Cheng, (2015). "Purification of coagulation factor VIII by immobilized metal affinity chromatography." Biotechnology and Applied Biochemistry, 62(3): 343-348.
Tamer, U., Gündoğdu, Y., Boyacı, İ. H. and K. Pekmez, (2010). "Synthesis of magnetic core–shell Fe3O4–Au nanoparticle for biomolecule immobilization and detection." Journal of Nanoparticle Research, 12(4): 1187-1196.
Turcheniuk, K., Tarasevych, A. V., Kukhar, V. P., Boukherroub, R. and S. Szunerits, (2013). "Recent advances in surface chemistry strategies for the fabrication of functional iron oxide based magnetic nanoparticles." Nanoscale, 5(22): 10729-10752.
Wang, L., Park, H. Y., Stephanie, I., Lim, I., Schadt, M. J., Mott, D., Luo, J., Wang, X. and C. J. Zhong, (2008). " Core@ shell nanomaterials: gold-coated magnetic oxide nanoparticles." Journal of Materials Chemistry, 18(23): 2629-2635.
Wang, W., Wang, Y. J. and D. N. Kelner, (2003). "Coagulation factor VIII: structure and stability." International Journal of Pharmaceutics, 259(1): 1-15.
Wang, Z., Zhao, J. C., Lian, H. Z. and H. Y. Chen, (2015). "Aptamer-based organic-silica hybrid affinity monolith prepared via "thiol-ene" click reaction for extraction of thrombin." Talanta, 138: 52-58. doi: 10.1016/j.talanta.2015.02.009
Wu, Y., Yang, X., Yi, X., Liu, Y. and Y. Chen, (2015). "Magnetic Nanoparticle for Biomedicine Applications." HSOA Journal of Nanotechnology: Nanomedicine and Nanobiotechnology, 2(1): 003.
Xu, J., Sun, J., Wang, Y., Sheng, J., Wang, F. and M. Sun, (2014). "Application of iron magnetic nanoparticles in protein immobilization."Molecules, 19(8): 11465-11486.
Yang, G., Wei, Q., Zhao, X. and F. Qu, (2016). "Research advances of aptamers selection for protein targets." Chinese Journal of Chromatography (SePu), 34(4): 370-381. doi: 10.3724/ SP.J.1123.2015.12014
Zeinali Sehrig, F., Majidi, S., Nikzamir, N., Nikzamir, N., Nikzamir, M. and A. Akbarzadeh, (2016). "Magnetic nanoparticles as potential candidates for biomedical and biological applications." Artificial Cells, Nanomedicine, and Biotechnology, 44(3): 918-927.
- Abstract Viewed: 738 times
- PDF Downloaded: 210 times