journal article·2012-11-28Open access

Dextran-Coated Magnetic Supports Modified with a Biomimetic Ligand for IgG Purification

Sara D. F. Santana, Vijaykumar L. Dhadge, Ana C.A. Roque

Abstract

Dextran-coated iron oxide magnetic particles modified with ligand 22/8, a protein A mimetic ligand, were prepared and assessed for IgG purification. Dextran was chosen as the agent to modify the surface of magnetic particles by presenting a negligible level of nonspecific adsorption. For the functionalization of the particles with the affinity ligand toward antibodies, three methods have been explored. The optimum coupling method yielded a theoretical maximum capacity for human IgG calculated as 568 ± 33 mg/g and a binding affinity constant of 7.7 × 10⁴ M⁻¹. Regeneration, recycle and reuse of particles was also highly successful for five cycles with minor loss of capacity. Moreover, this support presented specificity and effectiveness for IgG adsorption and elution at pH 11 directly from crude extracts with a final purity of 95% in the eluted fraction.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Monoclonal and Polyclonal Antibodies Research · Protein purification and stability · Nanoparticle-Based Drug Delivery

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal

References (37)

Show source-provided references
1. Wang W. · J. Pharm. Sci. · 2007 · 96 · 110.1002/jps.20727 ↗
2. Birch J. R. · Adv. Drug Delivery Rev. · 2006 · 58 · 67110.1016/j.addr.2005.12.006 ↗
3. Roque A. C. A. · J. Chromatogr., A · 2007 · 1160 · 4410.1016/j.chroma.2007.05.109 ↗
4. González Y. · J. Chromatogr., B · 2003 · 784 · 18310.1016/S1570-0232(02)00712-2 ↗
5. Kriangkum J. · Hybridoma · 2000 · 19 · 3310.1089/027245700315770 ↗
6. Powers D. B. · J. Immunol. Methods · 2001 · 251 · 12310.1016/S0022-1759(00)00290-8 ↗
7. Teng S. F. · J. Chromatogr., B: Biomed. Sci. Appl. · 2000 · 740 · 110.1016/S0378-4347(99)00549-6 ↗
8. Roque A. C. A. · J. Mol. Recognit. · 2005 · 18 · 21310.1002/jmr.733 ↗
9. Roque A. C. A. · J. Chromatogr., A · 2005 · 1064 · 15710.1016/j.chroma.2004.11.102 ↗
10. Branco R. J. F. · J. Chromatogr., A · 2012 · 1244 · 10610.1016/j.chroma.2012.04.071 ↗
11. Rosa P. A. J. · J. Biotechnol. · 2009 · 139 · 30610.1016/j.jbiotec.2009.01.001 ↗
12. Ditsch A. · Biotechnol. Prog. · 2006 · 22 · 115310.1021/bp050290t ↗
13. Laurent S. · Chem. Rev. · 2008 · 108 · 206410.1021/cr068445e ↗
14. Boyer C. · NPG Asia Mater. · 2010 · 2310.1038/asiamat.2010.6 ↗
15. Dias A. M. G. C. · Biotechnol. Adv. · 2011 · 29 · 14210.1016/j.biotechadv.2010.10.003 ↗
16. Lu A.-H. · Angew. Chem., Int. Ed. · 2007 · 46 · 122210.1002/anie.200602866 ↗
17. Dawes C. C. · Anal. Biochem. · 2005 · 338 · 18610.1016/j.ab.2004.12.010 ↗
18. Kievit F. M. · Adv. Funct. Mater. · 2009 · 19 · 224410.1002/adfm.200801844 ↗
19. Dung T. T. · J. Exp. Nanosci. · 2009 · 4 · 25910.1080/17458080802570609 ↗
20. Hradil J. · China Particuol. · 2007 · 5
21. Batalha I. L. · J. Mol. Recognit. · 2010 · 23 · 46210.1002/jmr.1013 ↗
22. Roque A. C. A. · J. Biotechnol. · 2009 · 144 · 31310.1016/j.jbiotec.2009.08.020 ↗
23. Kaittanis C. · PLoS ONE · 2008 · 3 · e325310.1371/journal.pone.0003253 ↗
24. Kaittanis C. · Adv. Drug Delivery Rev. · 2010 · 62 · 40810.1016/j.addr.2009.11.013 ↗
25. Heebøll-Nielsen A. · Biotechnol. Bioeng. · 2004 · 87 · 31110.1002/bit.20116 ↗
26. Heebøll-Nielsen A. · Sep. Sci. Technol. · 2004 · 39 · 289110.1081/SS-200028791 ↗
27. Huang X. · Langmuir · 2009 · 25 · 1165710.1021/la901258p ↗
28. Diettrich O. · FEBS Lett. · 1998 · 441 · 36910.1016/S0014-5793(98)01578-6 ↗
29. Duan H. · World J. Gastroenterol. · 2005 · 11 · 366010.3748/wjg.v11.i24.3660 ↗
30. Massart R. · IEEE Trans. Magn. · 1981 · 17 · 124710.1109/TMAG.1981.1061188 ↗
31. Leyva, A.; Quintana, A.; Sánchez, M.; Rodríguez, E. N.; Cremata, J.; Sánchez, J. C.Biologicals, 2008, 36,10.1016/j.biologicals.2007.09.001 ↗
32. Barroso T. · J. Membr. Sci. · 2010 · 348 · 22410.1016/j.memsci.2009.11.004 ↗
33. Sabaté R. · Int. J. Pharm. · 2008 · 347 · 15610.1016/j.ijpharm.2007.06.047 ↗
34. Williams D. · J. Nanopart. Res. · 2006 · 8 · 74910.1007/s11051-006-9084-7 ↗
35. Xu X. Q. · Appl. Surf. Sci. · 2005 · 252 · 49410.1016/j.apsusc.2005.01.027 ↗
36. Gupta A. K. · IEEE Trans. Nanobiosci. · 2004 · 3 · 6610.1109/TNB.2003.820277 ↗
37. Borlido L. · J. Chromatogr., A · 2011 · 1218 · 782110.1016/j.chroma.2011.08.084 ↗