An alternative assay to hydrophobic interaction chromatography for high-throughput characterization of monoclonal antibodies

mAbs

Volumn 7, Issue 3, 2015, Pages 553-561

  Estep, Patricia ^a   Caffry, Isabelle ^a   Yu, Yao ^a   Sun, Tingwan ^a   Cao, Yuan ^a   Lynaugh, Heather ^a   Jain, Tushar ^b   Vásquez, Maximiliano ^b   Tessier, Peter M ^c   Xu, Yingda ^a  

^a Protein Analytics Adimab   (United States)

^b Computational Biology Adimab ^*  (United States)

^c Rensselaer Polytechnic Institute   (United States)

Author keywords

Aggregation; Developability; HIC; High throughput screening; Hydrophobic interaction chromatography; Manufacturability; Self association; Self interaction nanoparticle spectroscopy; Solubility; Viscosity

Indexed keywords

ADALIMUMAB; AMMONIUM SULFATE; ANTIBODY CONJUGATE; BRODALUMAB; CANAKINUMAB; DACLIZUMAB; DENOSUMAB; FORALUMAB; FRESOLIMUMAB; GANITUMAB; GANTENERUMAB; GOLD NANOPARTICLE; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G1; IPILIMUMAB; MATUZUMAB; MONOCLONAL ANTIBODY; NECITUMUMAB; NIVOLUMAB; PANITUMUMAB; RADRETUMAB; RAMUCIRUMAB; TICILIMUMAB; TRASTUZUMAB; UNINDEXED DRUG; URELUMAB; USTEKINUMAB; VEDOLIZUMAB; VESENCUMAB; ZANOLIMUMAB; GOLD; METAL NANOPARTICLE;

AFFINITY CAPTURE SELF INTERACTION NANOPARTICLE SPECTROSCOPY; ARTICLE; BIOLOGICAL ACTIVITY; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; HEK293 CELL LINE; HIGH THROUGHPUT SCREENING; HUMAN; HUMAN CELL; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; HYDROPHOBICITY; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; SOLUBILITY; SPECTROSCOPY; VISCOSITY; CHEMICAL PHENOMENA; CHEMISTRY; LIQUID CHROMATOGRAPHY;

ANTIBODIES, MONOCLONAL; CHROMATOGRAPHY, LIQUID; GOLD; HEK293 CELLS; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; METAL NANOPARTICLES; SOLUBILITY; SPECTRUM ANALYSIS;

EID: 84945179967     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.1080/19420862.2015.1016694     Document Type: Article

References (22)

1. Reichert JM. Which are the antibodies to watch in 2013? MAbs 2013; 5: 1-4; PMID: 23254906; http://dx. doi. org/10. 4161/mabs. 22976.
2. Connolly BD, Petry C, Yadav S, Demeule B, Ciaccio N, Moore JM, Shire SJ, Gokarn YR. Weak interactions govern the viscosity of concentrated antibody solutions: highthroughput analysis using the diffusion interaction parameter. Biophys J 2012; 103: 69-78; PMID: 22828333; http://dx. doi. org/10. 1016/j. bpj. 2012. 04. 047.
3. Hotzel I, Theil FP, Bernstein LJ, Prabhu S, Deng R, Quintana L, Lutman J, Sibia R, Chan P, Bumbaca D, et al. A strategy for risk mitigation of antibodies with fast clearance. MAbs 2012; 4: 753-60; PMID: 23778268; http://dx. doi. org/10. 4161/mabs. 22189.
4. Perchiacca JM, Tessier PM. Engineering aggregationresistant antibodies. Annu Rev Chem Biomol Eng 2012; 3: 263-86; PMID: 22468604; http://dx. doi. org/10. 1146/annurev-chembioeng-062011-081052.
5. Shire SJ, Shahrokh Z, Liu J. Challenges in the development of high protein concentration formulations. J Pharm Sci 2004; 93: 1390-402; PMID: 15124199; http://dx. doi. org/10. 1002/jps. 20079.
6. Cromwell ME, Hilario E, Jacobson F. Protein aggregation and bioprocessing. AAPS J 2006; 8: E572-9; PMID: 17025275; http://dx. doi. org/10. 1208/aapsj 080366.
7. Geng SB, Cheung JK, Narasimhan C, Shameem M, Tessier PM. Improving monoclonal antibody selection and engineering using measurements of colloidal protein interactions. J Pharm Sci 2014; 103: 3356-63; PMID: 25209466; http://dx. doi. org/10. 1002/jps. 24130.
8. Tessier PM, WuJ, Dickinson CD. Emerging methods for identifying monoclonal antibodies with low propensity to self-associate during the early discovery process. Expert Opin Drug Deliv 2014; 11: 461-5; PMID: 24444112; http://dx. doi. org/10. 1517/17425247. 2014. 876989.
9. Tessier PM, Sandler SI, Lenhoff AM. Direct measurement of protein osmotic second virial cross coefficients by cross-interaction chromatography. Protein Sci 2004; 13: 1379-90; PMID: 15075404; http://dx. doi. org/10. 1110/ps. 03419204.
10. Jacobs SA, Wu SJ, Feng Y, Bethea D, O'Neil KT. Cross-interaction chromatography: a rapid method to identify highly soluble monoclonal antibody candidates. Pharm Res 2010; 27: 65-71; PMID: 19911257; http://dx. doi. org/10. 1007/s11095-009-0007-z.
11. Spencer S, Bethea D, Raju TS, Giles-Komar J, Feng Y. Solubility evaluation of murine hybridoma antibodies. MAbs 2012; 4: 319-25; PMID: 22531448; http://dx. doi. org/10. 4161/mabs. 19869.
12. Teske CA, Blanch HW, Prausnitz JM. Chromatographic measurement of interactions between unlike proteins. Fluid Phase Equilibr 2004; 219: 139-48; http://dx. doi. org/10. 1016/j. fluid. 2004. 01. 025.
13. Xu Y, Roach W, Sun T, Jain T, Prinz B, Yu TY, Torrey J, Thomas J, Bobrowicz P, Vasquez M, et al. Addressing polyspecificity of antibodies selected from an in vitro yeast presentation system: a FACS-based, highthroughput selection and analytical tool. Protein Eng Des Sel 2013; 26: 663-70; PMID: 24046438; http://dx. doi. org/10. 1093/protein/gzt047.
14. Liu Y, Caffry I, Wu J, Geng SB, Jain T, Sun T, Reid F, Cao Y, Estep P, Yu Y, et al. High-throughput screening for developability during early-stage antibody discovery using self-interaction nanoparticle spectroscopy. MAbs 2014; 6: 483-92; PMID: 24492294; http://dx. doi. org/10. 4161/mabs. 27431.
15. Sule SV, Dickinson CD, Lu J, Chow CK, Tessier PM. Rapid analysis of antibody self-association in complex mixtures using immunogold conjugates. Mol Pharm 2013; 10: 1322-31; PMID: 23383873; http://dx. doi. org/10. 1021/mp300524x.
16. Jayaraman J, wu J, Brunelle MC, Cruz AMM, Goldberg DS, Lobo BL, Shah A, Tessier PM. Plasmonic measurements of monoclonal antibody self-association using self-interaction nanoparticle spectroscopy. Biotechnol Bioeng 2014; 111(8): 1513-20; ePub Feb 20; PMID: 25097914.
17. To BC, Lenhoff AM. Hydrophobic interaction chromatography of proteins. II. Solution thermodynamic properties as a determinant of retention. J Chromatogr A 2007; 1141: 235-43; PMID: 17207494; http://dx. doi. org/10. 1016/j. chroma. 2006. 12. 022.
18. Yamniuk AP, Ditto N, Patel M, Dai J, Sejwal P, Stetsko P, Doyle ML. Application of a kosmotrope-based solubility assay to multiple protein therapeutic classes indicates broad use as a high-throughput screen for protein therapeutic aggregation propensity. J Pharm Sci 2013; 102: 2424-39; PMID: 23712759; http://dx. doi. org/10. 1002/jps. 23618.
19. Nfor BK, Hylkema NN, Wiedhaup KR, Verhaert PD, van der Wielen LA, Ottens M. High-throughput protein precipitation and hydrophobic interaction chromatography: salt effects and thermodynamic interrelation. J Chromatogr A 2011; 1218: 8958-73; PMID: 21868020; http://dx. doi. org/10. 1016/j. chroma. 2011. 08. 016.
20. Gagnon P, Mayes T, Danielsson A. An adaptation of hydrophobic interaction chromatography for estimation of protein solubility optima. J Pharm Biomed Anal 1997; 16: 587-92; PMID: 9502154; http://dx. doi. org/10. 1016/S0731-7085(97)00153-2.
21. Berkowitz SA, Henry MP. Use of high-performance hydrophobic interaction chromatography for the determination of salting-out conditions of proteins. J Chromatogr 1987; 389: 317-21; PMID: 3571359; http://dx. doi. org/10. 1016/S0021-9673(01)94441-3.
22. Haverick M, Mengisen S, Shameem M, Ambrogelly A. Separation of mAbs molecular variants by analytical hydrophobic interaction chromatography HPLC: overview and applications. Mabs; 6(4): 852-8; PMID: 24751784; http://dx. doi. org/10. 4161/mabs. 28693.