Hostname: page-component-7479d7b7d-fwgfc Total loading time: 0 Render date: 2024-07-10T23:34:33.587Z Has data issue: false hasContentIssue false
  • English
  • Français

Nickel nanoparticles synthesized by a modified polyol method for the purification of histidine-tagged single-domain antibody ToxA5.1

Published online by Cambridge University Press:  17 October 2012

Albert Parisien ,
Fady Al-Zarka ,
Greg Hussack ,
Elena A. Baranova ,
Jules Thibault  and
Christopher Qingdao Lan
Albert Parisien
Affiliation:
Department of Chemical and Biological Engineering, University of Ottawa, Ottawa, Ontario, Canada K1N 6N5
Fady Al-Zarka
Affiliation:
Department of Chemical and Biological Engineering, University of Ottawa, Ottawa, Ontario, Canada K1N 6N5
Greg Hussack
Affiliation:
Institute for Biological Sciences, National Research Council Canada, Ottawa, Ontario, Canada K1A 0R6
Elena A. Baranova
Affiliation:
Department of Chemical and Biological Engineering, University of Ottawa, Ottawa, Ontario, Canada K1N 6N5
Jules Thibault
Affiliation:
Department of Chemical and Biological Engineering, University of Ottawa, Ottawa, Ontario, Canada K1N 6N5
Christopher Qingdao Lan*
Affiliation:
Department of Chemical and Biological Engineering, University of Ottawa, Ottawa, Ontario, Canada K1N 6N5
*
a)Address all correspondence to this author. e-mail: Christopher.Lan@uottawa.ca
Get access

Abstract

Nickel nanoparticles (NNPs) synthesized by a modified polyol method using ethylene glycol as a reducing agent, palladium chloride as a nucleating agent, and polyvinylpyrrolidone (PVP) as a protective agent were investigated as a potential magnetic adsorbent for the purification of hexahistidine-tagged (His6-tagged) recombinant proteins. The synthesis resulted in nanoparticles having an average diameter of 68 ± 28 nm. The x-ray diffraction pattern confirmed the presence of nickel metal, as well as the presence of unreacted nickel (II) hydroxide Ni(OH)2. Magnetic characterization showed that a magnetization saturation of 39.3 electromagnetic unit (emu)/g at 20,000 Oersted (Oe) was reached rapidly and that the material exhibited ferromagnetic behavior. Protein purification results showed that the synthesized NNPs were highly selective for binding to a His6-tagged recombinant protein single-domain antibody ToxA5.1. In addition, NNPs were used for four adsorption cycles without significant binding capacity losses. These particles have shown great potential such as being easily synthesized, cost-effective, and highly selective magnetic adsorbents for the purification of His6-tagged recombinant proteins.

Keywords

magneticadsorptionpurification
Type
Articles
Information
Journal of Materials Research , Volume 27 , Issue 22 , 22 November 2012 , pp. 2884 - 2890
Copyright
Copyright © Materials Research Society 2012

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Langer, E. and Ranck, J.: Capacity bottleneck squeezed by downstream processes. Bioprocess Int. 4, 14 (2006).Google Scholar
Low, D., O’Leary, R., and Pujar, N.S.: Future of antibody purification. J. Chromatogr. B 848, 48 (2007).CrossRefGoogle ScholarPubMed
Franzreb, M., Siemann-Herzberg, M., Hobley, T.J., and Thomas, O.R.T.: Protein purification using magnetic adsorbent particles. Appl. Microbiol. Biotechnol. 70, 505 (2006).CrossRefGoogle ScholarPubMed
Horák, D., Babič, M., Macková, H., and Beneš, M.J.: Preparation and properties of magnetic nano- and microsized particles for biological and environmental separations. J. Sep. Sci. 30, 1751 (2007).CrossRefGoogle ScholarPubMed
Ai, F., Yao, A., Huang, W., Wang, D., and Zhang, X.: Synthesis of PVP-protected NiPd nanoalloys by modified polyol process and their magnetic properties. Physica E 42, 1281 (2010).CrossRefGoogle Scholar
Couto, G.G., Klein, J.J., Schreiner, W.H., Mosca, D.H., de Oliveira, A.J.A., and Zarbin, A.J.G.: Nickel nanoparticles obtained by a modified polyol process: Synthesis, characterization, and magnetic properties. J. Colloid Interface Sci. 311, 461 (2007).CrossRefGoogle ScholarPubMed
Zhang, H., Ding, J., Chow, G., Ran, M., and Yi, J.: Engineering magnetic properties of Ni nanoparticles by nonmagnetic cores. Chem. Mater. 21, 5222 (2009).CrossRefGoogle Scholar
Porath, J. and Olin, B.: Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ions. Biochemistry 22, 1621 (1983).CrossRefGoogle ScholarPubMed
Porath, J.: Immobilized metal ion affinity chromatography. Protein Expression Purif. 3, 263 (1992).CrossRefGoogle ScholarPubMed
Carroll, K.J., Reveles, J.U., Shultz, M.D., Khanna, S.N., and Carpenter, E.E.: Preparation of elemental Cu and Ni nanoparticles by the polyol method: An experimental and theoretical approach. J. Phys. Chem. C 115, 2656 (2011).CrossRefGoogle Scholar
Baranova, E.A., Cally, A., Allagui, A., Ntais, S., and Wüthrich, R.: Nickel particles with increased catalytic activity towards hydrogen evolution reaction. C.R. Chim. (2012). doi: 10.1016/j.crci.2012.02.003.Google Scholar
Lee, I.S., Lee, N., Park, J., Kim, B.H., Yi, Y.W., Kim, T., Kim, T.K., Lee, I.H., Paik, S.R., and Hyeon, T.: Ni/NiO core/shell nanoparticles for selective binding and magnetic separation of histidine-tagged proteins. J. Am. Chem. Soc. 128, 10658 (2006).CrossRefGoogle ScholarPubMed
Kim, J., Piao, Y., Lee, N., Park, Y.I., Lee, I.H., Lee, J.H., Paik, S.R., and Hyeon, T.: Magnetic nanocomposite spheres decorated with NiO nanoparticles for a magnetically recyclable protein separation system. Adv. Mater. 22, 57 (2010).CrossRefGoogle ScholarPubMed
Bai, L., Fan, J., Cao, Y., Yuan, F., Zuo, A., and Tang, Q.: Shape-controlled synthesis of Ni particles via polyol reduction. J. Cryst. Growth 311, 2474 (2009).CrossRefGoogle Scholar
Hussack, G., Arbabi-Ghahroudi, M., Van Faassen, H., Songer, J.G., Ng, K.K.S., MacKenzie, R., and Tanha, J.: Neutralization of Clostridium difficile toxin A with single-domain antibodies targeting the cell receptor binding domain. J. Biol. Chem. 286, 8961 (2011).CrossRefGoogle ScholarPubMed
Abràmoff, M.D., Magalhães, P.J., and Ram, S.J.: Image processing with imageJ. Biophotonics Int. 11, 36 (2004).Google Scholar
Laemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680 (1970).CrossRefGoogle ScholarPubMed
Cullity, B.D.: Elements of X-Ray Diffraction, 3rd ed. (Addison-Wesley Publishing Co., Boston, MA, 1956).Google Scholar
Chou, K.S. and Huang, K.C.: Studies on the chemical synthesis of nanosized nickel powder and its stability. J. Nanopart. Res. 3, 127 (2001).CrossRefGoogle Scholar
West, A.R.: Solid State Chemistry and its Applications (Wiley, Hoboken, NJ, 1984).Google Scholar
Gaberc-Porekar, V. and Menart, V.: Perspectives of immobilized-metal affinity chromatography. J. Biochem. Bioph. Methods 49, 335 (2001).CrossRefGoogle ScholarPubMed
Block, H., Maertens, B., Spriestersbach, A., Brinker, N., Kubicek, J., Fabis, R., Labahn, J., and Schäfer, F.: Immobilized-metal affinity chromatography (IMAC). A review, in Methods in Enzymology (Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany, 2009), p. 439.Google Scholar
Chen, C.W., Liu, H.L., Lin, J.C., and Ho, Y.: Molecular dynamics simulations of metal ion binding to the His-tag motif. J. Chin. Chem. Soc. 52, 1281 (2005).CrossRefGoogle Scholar
Nam, J.M., Han, S.W., Lee, K.B., Liu, X., Ratner, M.A., and Mirkin, C.A.: Bioactive protein nanoarrays on nickel oxide surfaces formed by dip-pen nanolithography. Angew. Chem. Int. Ed. 43, 1246 (2004).CrossRefGoogle ScholarPubMed