Avoiding antibody aggregation during processing: Establishing hold times

Biotechnology Journal

Volumn 9, Issue 9, 2014, Pages 1195-1205

  Joshi, Varsha ^a   Shivach, Tarun ^a   Kumar, Vijesh ^a   Yadav, Nitin ^a   Rathore, Anurag ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY DELHI   (India)

Author keywords

Aggregation; Charged variants; Immunoglobulin; Regression analysis; Stability

Indexed keywords

AFFINITY CHROMATOGRAPHY; AGGLOMERATION; AMINO ACIDS; CHROMATOGRAPHIC ANALYSIS; CONVERGENCE OF NUMERICAL METHODS; MONOCLONAL ANTIBODIES; REGRESSION ANALYSIS; VOLATILE FATTY ACIDS;

ANION EXCHANGE CHROMATOGRAPHY; CATION EXCHANGE CHROMATOGRAPHY; CHARGED VARIANTS; IMMUNOGLOBULIN; ION-EXCHANGE CHROMATOGRAPHY; LEAST SQUARES REGRESSION; MANUFACTURING CONDITIONS; MONOCLONAL ANTIBODIES (MAB);

MANUFACTURE;

BUFFER; IMMUNOGLOBULIN; MONOCLONAL ANTIBODY;

CHEMISTRY; CIRCULAR DICHROISM; ION EXCHANGE CHROMATOGRAPHY; PH; PROCEDURES;

ANTIBODIES, MONOCLONAL; BUFFERS; CHROMATOGRAPHY, ION EXCHANGE; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; IMMUNOGLOBULINS;

EID: 84906821537     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201400052     Document Type: Article

References (40)

1. Rosa, P. A., Ferreira, I. F., Azevedo, A. M., Aires-Barros, M. R., Aqueous two-phase systems: A viable platform in the manufacturing of biopharmaceuticals. J. Chromatogr. A 2010, 1217, 2296-2305.
2. Walsh, G., Biopharmaceutical benchmarks 2010. Nat. Biotechnol. 2010, 28, 917.
3. De Groot, A. S., Scott, D. W., Immunogenicity of protein therapeutics. Trends Immunol. 2007, 28, 482-490.
4. Arosio, P., Barolo, G., Müller-Späth, T., Wu, H., Morbidelli, M., Aggregation stability of a monoclonal antibody during downstream processing. Pharm. Res. 2011, 28, 1884-1894.
5. De Bernardez Clark, E., Schwarz, E., Rudolph, R., Inhibition of aggregation side reactions during in vitro protein folding. Methods Enzymol. 1999, 309, 217-236.
6. Rosenberg, A. S., Effects of protein aggregates: An immunologic perspective. AAPS J. 2006, 8, E501-E507.
7. Levine, H., Jagschies, G., The Development of Therapeutic Monoclonal Antibody Products: A Comprehensive Guide to CMC Activities From Clone to Clinic, BioProcess Consultants 2010.
8. Brummitt, R. K., Nesta, D. P., Chang, L., Chase, S. F. et al., Nonnative aggregation of an IgG1 antibody in acidic conditions: Part 1. Unfolding, colloidal interactions, and formation of high-molecular-weight aggregates. J. Pharm. Sci. 2011, 100, 2087-2103.
9. Hari, S. B., Lau, H., Razinkov, V. I., Chen, S., Latypov, R. F., Acid-induced aggregation of human monoclonal IgG1 and IgG2: Molecular mechanism and the effect of solution composition. Biochemistry 2010, 49, 9328-9338.
10. Chi, E. Y., Krishnan, S., Randolph, T. W., Carpenter, J. F., Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation. Pharm. Res. 2003, 20, 1325-1336.
11. Vázquez-Rey, M., Lang, D. A., Aggregates in monoclonal antibody manufacturing processes. Biotechnol. Bioeng. 2011, 108, 1494-1508.
12. Rathore, A. S., Follow-on protein products: Scientific issues, developments and challenges. Trends Biotechnol. 2009, 27, 698-705.
13. Carson, K. L., Flexibility-the guiding principle for antibody manufacturing. Nat. Biotechnol. 2005, 23, 1054-1058.
14. Cleland, J. L., Powell, M. F., Shire, S. J., The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation. Crit. Rev. Ther. Drug Carrier Syst. 1992, 10, 307-377.
15. Manning, M. C., Patel, K., Borchardt, R. T., Stability of protein pharmaceuticals. Pharm. Res. 1989, 6, 903-918.
16. Harris, R. J., Shire, S. J., Winter, C., Commercial manufacturing scale formulation and analytical characterization of therapeutic recombinant antibodies. Drug Dev. Res. 2004, 61, 137-154.
17. Wang, W., Singh, S., Zeng, D. L., King, K., Nema, S., Antibody structure, instability, and formulation. J. Pharm. Sci. 2007, 96, 1-26.
18. He, X. Z., Que, A. H., Mo, J. J., Analysis of charge heterogeneities in mAbs using imaged CE. Electrophoresis 2009, 30, 714-722.
19. Sharifi, J., Khawli, L., Hornick, J., Epstein, A., Improving monoclonal antibody pharmacokinetics via chemical modification. Q. J. Nucl. Med. 1998, 42, 242.
20. Igawa, T., Tsunoda, H., Tachibana, T., Maeda, A. et al., Reduced elimination of IgG antibodies by engineering the variable region. Protein Eng. Des. Sel. 2010, 23, 385-392.
21. Shukla, A. A., Hubbard, B., Tressel, T., Guhan, S., Low, D., Downstream processing of monoclonal antibodies-application of platform approaches. J. Chromatogr. B 2007, 848, 28-39.
22. Shukla, A. A., Thömmes, J., Recent advances in large-scale production of monoclonal antibodies and related proteins. Trends Biotechnol. 2010, 28, 253-261.
23. Rathore, A. S., Kumar, V., Tugcu, N., Godavarti, R., Evolution of the monoclonal antibody platform. BioPharm Int. 2013, 26, 32-37.
24. Vermeer, A. W., Norde, W., The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein. Biophys. J. 2000, 78, 394-404.
25. Calmettes, P., Cser, L., Rajnavölgyi, Temperature and pH dependence of immunoglobulin G conformation. Arch. Biochem. Biophys. 1991, 291, 277-283.
26. Arakawa, T., Philo, J. S., Tsumoto, K., Yumioka, R., Ejima, D., Elution of antibodies from a Protein-A column by aqueous arginine solutions. Protein Expr. Purif. 2004, 36, 244-248.
27. Arakawa, T., Philo, J. S., Ejima, D., Tsumoto, K., Arisaka, F., Aggregation analysis of therapeutic proteins, part 1. BioProcess Int. 2006, 4, 32-42.
28. Pace, C. N., Conformational stability of globular proteins. Trends Biochem. Sci. 1990, 15, 14-17.
29. Pedersen, J. T., Heegaard, N. H., Analysis of protein aggregation in neurodegenerative disease. Anal. Chem. 2013, 85, 4215-4227.
30. Josic, D., Lim, Y.-P., Analytical and preparative methods for purification of antibodies. Food Technol. Biotechnol. 2001, 39, 215-226.
31. Kelly, S. M., Jess, T. J., Price, N. C., How to study proteins by circular dichroism. Biochim. Biophys. Acta 2005, 1751, 119-139.
32. Kumar, V., Bhalla, A., Rathore, A. S., Design of experiments applications in bioprocessing: Concepts and approach. Biotechnol. Prog. 2013, 30, 86-99.
33. Liu, H. F., Ma, J., Winter, C., Bayer, R., Recovery and purification process development for monoclonal antibody production. MAbs 2010, 2, 480-499.
34. Vermeer, A. W., Bremer, M. G., Norde, W., Structural changes of IgG induced by heat treatment and by adsorption onto a hydrophobic Teflon surface studied by circular dichroism spectroscopy. Biochim. Biophys. Acta 1998, 1425, 1-12.
35. Chen, S., Lau, H., Brodsky, Y., Kleemann, G. R., Latypov, R. F., The use of native cation-exchange chromatography to study aggregation and phase separation of monoclonal antibodies. Protein Sci. 2010, 19, 1191-1204.
36. Lajmi, A. R., Nochumson, S., Berges, A., Impact of antibody aggregation on a flowthrough anion-exchange membrane process. Biotechnol. Prog. 2010, 26, 1654-1661.
37. Harn, N., Allan, C., Oliver, C., Middaugh, C., Highly concentrated monoclonal antibody solutions: direct analysis of physical structure and thermal stability. J. Pharm. Sci. 2007, 96, 532-546.
38. Khawli, L. A., Goswami, S., Hutchinson, R., Kwong, Z. W. et al., Charge variants in IgG1: Isolation, characterization, in vitro binding properties and pharmacokinetics in rats. MAbs 2010, 2, 613-624.
39. Alvarez, M., Tremintin, G., Wang, J., Eng, M. et al., On-line characterization of monoclonal antibody variants by liquid chromatography-mass spectrometry operating in a two-dimensional format. Anal. Biochem. 2011, 419, 17-25.
40. Vlasak, J., Ionescu, R., Heterogeneity of monoclonal antibodies revealed by charge-sensitive methods. Curr. Pharm. Biotechnol. 2008, 9, 468-481.