Streamlined process development procedure incorporating the selection of various stationary phase types established in a mAb aggregate reduction study with different mixed mode ligands.
aggregate removal
high throughput screening
mixed mode chromatography
platform development
Journal
Biotechnology progress
ISSN: 1520-6033
Titre abrégé: Biotechnol Prog
Pays: United States
ID NLM: 8506292
Informations de publication
Date de publication:
03 2022
03 2022
Historique:
revised:
10
12
2021
received:
22
08
2021
accepted:
28
12
2021
pubmed:
31
12
2021
medline:
23
4
2022
entrez:
30
12
2021
Statut:
ppublish
Résumé
In biopharmaceutical process development time, cost and reliability are the relevant keywords. During the development of chromatographic processes these targets are challenged by many possible scaffolds, ligands and process parameters. The common response to this diversity is the establishment of platform processes in the development of chromatographic unit operations. However, while developing a platform library to simplify and accelerate chromatographic processes, the potential combination of scaffold, ligands and process parameters need to be characterized. This challenge is addressed in a case study on novel mixed mode (MM) adsorber for the removal of monoclonal antibody (mAb) aggregates. We propose a rigorous strategy to reduce the various experimental design space resulting from possible combinations in scaffolds, backbones and ligands. This strategy is based on theoretical considerations, identification of adsorber selectivity and capacity for the identification of a suitable membrane system. For this system, each potential MM membrane adsorber candidate is investigated in its high molecular weight species reduction potential for a given mAb feed stream and referenced to the performance of Capto™ Adhere. The introduced strategy can reduce the developmental effort in an early stage from three to two possible stationary phases. Thereafter, initial examinations at different ionic capacities enlighten one favorable stationary phase. Finalizing the development strategy procedure by studying five different MM ligands by HTS and confirming the study with a 2-3 MV higher dynamic breakthrough capacity in benchtop experiments and provides an insight in the benefits of a living process platform library.
Substances chimiques
Antibodies, Monoclonal
0
Ligands
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e3230Informations de copyright
© 2021 American Institute of Chemical Engineers.
Références
Keller WR, Evans ST, Ferreira G, Robbins D, Cramer SM. Use of MiniColumns for linear isotherm parameter estimation and prediction of benchtop column performance. J Chromatogr A. 2015;1418:94-102. doi:10.1016/j.chroma.2015.09.038
Coffman JL, Kramarczyk JF, Kelley BD. High-throughput screening of chromatographic separations: I. method development and column modeling. Biotechnol Bioeng. 2008;100(4):605-618. doi:10.1002/bit.21904
Lye G, Hubbuch J, Schroeder T, Willimann E. Shrinking the costs of bioprocess development case study automation; 2009;October:18-22.
Shukla AA, Thömmes J. Recent advances in large-scale production of monoclonal antibodies and related proteins. Trends Biotechnol. 2010;28(5):253-261. doi:10.1016/j.tibtech.2010.02.001
Gottschalk U, ed. Process Scale Purification of Antibodies. 2nd ed. John Wiley & Sons Inc; 2017. doi:10.1002/9781119126942
Gottschalk U, Brorson K, Shukla AA. Innovation in biomanufacturing: the only way forward. Pharmaceut Bioprocess. 2013;1(2):141-157. doi:10.4155/pbp.13.17
Wolfe LS, Barringer CP, Mostafa SS, Shukla AA. Multimodal chromatography: characterization of protein binding and selectivity enhancement through mobile phase modulators. J Chromatogr A. 2014;1340:151-156. doi:10.1016/j.chroma.2014.02.086
www.efpia.eu. 2018: The pharmaceutical industry in figures. Accessed May 31, 2020. https://efpia.eu/publications/downloads/efpia/2018-the-pharmaceutical-industry-in-figures/
F. Hoffmann-La Roche AG. Roche Product Development Portfolio. Updated February 13, 2020. Accessed February 13, 2020. https://www.roche.com/de/research_and_development/who_we_are_how_we_work/pipeline.htm
AbbVie. abbvie Pipeline. Accessed February 13, 2020. https://www.abbvie.com/our-science/pipeline.html
GlaxoSmithKline plc. Our pipeline | GSK. Accessed February 13, 2020. https://www.gsk.com/en-gb/research-and-development/our-pipeline/.
Novartis International AG. Novartis Global Pipeline | Novartis. Accessed February 13, 2020. https://www.novartis.com/our-science/novartis-global-pipeline?field_pipeline_therapeutic_area=2121&field_pipeline_therapeutic_area=2616&field_pipeline_therapeutic_area=2126&field_pipeline_therapeutic_area=2131&field_pipeline_therapeutic_area=2136&field_pipeline_therapeutic_area=2141&field_pipeline_therapeutic_area=2146&field_pipeline_therapeutic_area=2151&field_pipeline_filing_date=All
Pfizer Inc. Product Pipeline | Pfizer. Updated February 13, 2020. Accessed February 13, 2020. https://www.pfizer.com/science/drug-product-pipeline
SANOFI. Product Pipeline SANOFI. Updated February 13, 2020. Accessed February 13, 2020. https://www.sanofi.com/en/science-and-innovation/research-and-development
Shukla AA, Hubbard B, Tressel T, Guhan S, Low D. Downstream processing of monoclonal antibodies--application of platform approaches. J Chromatogr B Analyt Technol Biomed Life Sci. 2007;848(1):28-39. doi:10.1016/j.jchromb.2006.09.026
Liu HF, Ma J, Winter C, Bayer R. Recovery and purification process development for monoclonal antibody production. MAbs. 2010;2(5):480-499. doi:10.4161/mabs.2.5.12645
Zhou JX, Tressel T. Basic concepts in Q membrane chromatography for large-scale antibody production. Biotechnol Prog. 2006;22(2):341-349. doi:10.1021/bp050425v
Knudsen HL, Fahrner RL, Xu Y, Norling LA, Blank GS. Membrane ion-exchange chromatography for process-scale antibody purification. J Chromatogr A. 2001;907(1-2):145-154. doi:10.1016/s0021-9673(00)01041-4
Kuczewski M, Fraud N, Faber R, Zarbis-Papastoitsis G. Development of a polishing step using a hydrophobic interaction membrane adsorber with a PER.C6-derived recombinant antibody. Biotechnol Bioeng. 2010;105(2):296-305. doi:10.1002/bit.22538
Dieter Melzner. New HIC and AEX membrane Adsorber; September 6, 2009; Montpellier, France.
Teepakorn C, Fiaty K, Charcosset C. Comparison of membrane chromatography and monolith chromatography for Lactoferrin and bovine serum albumin separation. Processes. 2016;4(3):31. doi:10.3390/pr4030031
Avallin J, Nilsson A, Asplund M, Pettersson N, Searle T, Jägersten C. Columns up to 1600 mm in diameter packed with protein A chromatography medium using axial mechanical compression. Accessed May 11, 2020. http://www.processdevelopmentforum.com/posters/columns-up-to-1600-mm-in-diameter-packed-with-protein-a-chromatography-medium-using-axial-mechanical-compression/.
Lenhoff AM. Protein adsorption and transport in polymer-functionalized ion-exchangers. J Chromatogr A. 2011;1218(49):8748-8759. doi:10.1016/j.chroma.2011.06.061
Schmoldt A, Benthe HF, Haberland G. Digitoxin metabolism by rat liver microsomes. Biochem Pharmacol. 1975;24(17):1639-1641.
Specht R, Han B, Wickramasinghe SR, et al. Densonucleosis virus purification by ion exchange membranes. Biotechnol Bioeng. 2004;88(4):465-473. doi:10.1002/bit.20270
Hunter AK, Carta G. Protein adsorption on novel acrylamido-based polymeric ion-exchangers. J Chromatogr A. 2000;897(1-2):65-80. doi:10.1016/S0021-9673(00)00864-5
Hunter AK, Carta G. Protein adsorption on novel acrylamido-based polymeric ion-exchangers. J Chromatogr A. 2002;971(1-2):105-116. doi:10.1016/S0021-9673(02)01027-0
Švec F, Tennikova TB, Deyl Z. Monolithic Materials: Preparation, Properties, and Applications. 1st ed. Elsevier; 2003. 67. http://www.sciencedirect.com/science/bookseries/03014770.
Müller E. Properties and characterization of high capacity resins for biochromatography. Chem Eng Technol. 2005;28(11):1295-1305. doi:10.1002/ceat.200500161
Orr V, Zhong L, Moo-Young M, Chou CP. Recent advances in bioprocessing application of membrane chromatography. Biotechnol Adv. 2013;31(4):450-465. doi:10.1016/j.biotechadv.2013.01.007
Yu M, Li Y, Zhang S, et al. Improving stability of virus-like particles by ion-exchange chromatographic supports with large pore size: advantages of gigaporous media beyond enhanced binding capacity. J Chromatogr A. 2014;1331:69-79. doi:10.1016/j.chroma.2014.01.027
Strancar A, Podgornik A, Barut M, Necina R. Short monolithic columns as stationary phases for biochromatography. Adv Biochem Eng Biotechnol. 2002;76:49-85. doi:10.1007/3-540-45345-8_2
BIA Separations d.o.o. Architecture of chromatography media and devices - BIA Separations. Accessed May 12, 2020. https://www.biaseparations.com/en/technology/architecture-of-chromatography-media-and-devices
Díaz-Bao M, Barreiro R, Miranda J, Cepeda A, Regal P. Recent advances and uses of monolithic columns for the analysis of residues and contaminants in food. Chromatography. 2015;2(1):79-95. doi:10.3390/chromatography2010079
Giese RW. Editorial on "Polymethacrylate monoliths for preparative and industrial separation of biomolecular assemblies" by a. Jungbauer and R. Hahn. J Chromatogr A. 2008;1184(1-2):61. doi:10.1016/j.chroma.2007.12.057
Schwellenbach J, Zobel S, Taft F, Villain L, Strube J. Purification of monoclonal antibodies using a fiber based cation-exchange stationary phase: parameter determination and modeling. Bioengineering. 2016;3(4):24. doi:10.3390/bioengineering3040024
Cytiva. HiTrap Fibro PrismA units - Cytiva. Accessed June 1, 2020. https://www.cytivalifesciences.com/en/us/shop/chromatography/membranes/hitrap-hiscreen-fibro-prisma-units-for-research-and-process-development-p-23550#related-documents.
Nelson DM, Stanelle RD, Brown P, Marcus RK. Capillary-Channeled Polymer (C-CP) fibers: a novel platform for liquid-phase separations; Accessed June 1, 2020. https://www.americanlaboratory.com/913-Technical-Articles/19170-Capillary-Channeled-Polymer-C-CP-Fibers-A-Novel-Platform-for-Liquid-Phase-Separations/
Charcosset C. Membrane chromatography. In: Charcosset C, ed. Membrane Chromatography. Elsevier; 2012:169-212.
Schwellenbach J, Kosiol P, Sölter B, Taft F, Villain L, Strube J. Controlling the polymer-nanolayer architecture on anion-exchange membrane adsorbers via surface-initiated atom transfer radical polymerization. React Funct Polym. 2016;106:32-42. doi:10.1016/j.reactfunctpolym.2016.07.005
Hardin AM, Harinarayan C, Malmquist G, Axén A, van Reis R. Ion exchange chromatography of monoclonal antibodies: effect of resin ligand density on dynamic binding capacity. J Chromatogr A. 2009;1216(20):4366-4371. doi:10.1016/j.chroma.2008.08.047
Sýkora D, Řezanka P, Záruba K, Král V. Recent advances in mixed-mode chromatographic stationary phases. J Sep Sci. 2019;42(1):89-129. doi:10.1002/jssc.201801048
Zhang K, Liu X. Mixed-mode chromatography in pharmaceutical and biopharmaceutical applications. J Pharm Biomed Anal. 2016;128:73-88. doi:10.1016/j.jpba.2016.05.007
Yang Y, Geng X. Mixed-mode chromatography and its applications to biopolymers. J Chromatogr A. 2011;1218(49):8813-8825. doi:10.1016/j.chroma.2011.10.009
Washburn MP, Wolters D, Yates JR. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol. 2001;19(3):242-247. doi:10.1038/85686
Link AJ, Eng J, Schieltz DM, et al. Direct analysis of protein complexes using mass spectrometry. Nat Biotechnol. 1999;17(7):676-682. doi:10.1038/10890
Toueille M, Uzel A, Depoisier J-F, Gantier R. Designing new monoclonal antibody purification processes using mixed-mode chromatography sorbents. J Chromatogr B Analyt Technol Biomed Life Sci. 2011;879(13-14):836-843. doi:10.1016/j.jchromb.2011.02.047
Voitl A, Müller-Späth T, Morbidelli M. Application of mixed mode resins for the purification of antibodies. J Chromatogr A. 2010;1217(37):5753-5760. doi:10.1016/j.chroma.2010.06.047
Wang J, Jenkins EW, Robinson JR, Wilson A, Husson SM. A new multimodal membrane adsorber for monoclonal antibody purifications. J Membr Sci. 2015;492:137-146. doi:10.1016/j.memsci.2015.05.013
Pezzini J, Joucla G, Gantier R, et al. Antibody capture by mixed-mode chromatography: a comprehensive study from determination of optimal purification conditions to identification of contaminating host cell proteins. J Chromatogr A. 2011;1218(45):8197-8208. doi:10.1016/j.chroma.2011.09.036
Kallberg K, Johansson H-O, Bulow L. Multimodal chromatography: an efficient tool in downstream processing of proteins. Biotechnol J. 2012;7(12):1485-1495. doi:10.1002/biot.201200074
Kaleas KA, Schmelzer CH, Pizarro SA. Industrial case study: evaluation of a mixed-mode resin for selective capture of a human growth factor recombinantly expressed in E. coli. J Chromatogr A. 2010;1217(2):235-242. doi:10.1016/j.chroma.2009.07.023
Alpert AJ. Electrostatic repulsion hydrophilic interaction chromatography for isocratic separation of charged solutes and selective isolation of phosphopeptides. Anal Chem. 2008;80(1):62-76. doi:10.1021/ac070997p
Kistler C, Pollard J, Ng LS, Streefland M. High-throughput bioprocess development. Genetic Eng Biotechnol News. 2016;36(7):30-31. doi:10.1089/gen.36.07.15
Wiendahl M, Schulze Wierling P, Nielsen J, et al. High throughput screening for the design and optimization of chromatographic processes: miniaturization, automation and parallelization of breakthrough and elution studies. Chem Eng Technol. 2008;31(6):893-903. doi:10.1002/ceat.200800167
Bensch M, Schulze Wierling P, von Lieres E, Hubbuch J. High throughput screening of chromatographic phases for rapid process development. Chem Eng Technol. 2005;28(11):1274-1284. doi:10.1002/ceat.200500153
Stein D, Thom V, Hubbuch J. High throughput screening setup of a scale-down device for membrane chromatography-aggregate removal of monoclonal antibodies. Biotechnology Progress. 2020;36(6):e3055. doi:10.1002/btpr.3055
Stein D, Thom V, Hubbuch J. Process development exploiting competitive adsorption-based displacement effects in monoclonal antibody aggregate removal-A new high-throughput screening procedure for membrane chromatography. Biotechnology and Applied Biochemistry. 2021. doi:10.1002/bab.2236
Vázquez-Rey M, Lang DA. Aggregates in monoclonal antibody manufacturing processes. Biotechnol Bioeng. 2011;108(7):1494-1508. doi:10.1002/bit.23155
Cromwell MEM, Hilario E, Jacobson F. Protein aggregation and bioprocessing. AAPS J. 2006;8(3):9. doi:10.1208/aapsj080366
Chi EY, Krishnan S, Randolph TW, Carpenter JF. Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation. Pharm Res. 2003;20(9):1325-1336. doi:10.1023/A:1025771421906
GE Healthcare. Capto adhere multimodal chromatography resin: GE Healthcare Life Sciences. Accessed February 3, 2020. https://www.gelifesciences.com/en/us/shop/chromatography/resins/multimodal/capto-adhere-multimodal-chromatography-resin-p-05643#tech-spec-table
GE Healthcare. Process development HiScreen™ prepacked columns. Accessed February 3, 2020. https://www.gelifesciences.com/en/us/shop/chromatography/prepacked-columns/multimodal/hiscreen-capto-adhere-p-00615#related-documents
GE Healthcare. Purification of monoclonal antibodies using modern chromatography media and membranes: 29094443 AB. Accessed February 3, 2020.