Separation of mAbs molecular variants by analytical hydrophobic interaction chromatography HPLC: overview and applications

References

• Ambrogelly A, Palioura S, Söll D. Natural expansion of the genetic code. Nat Chem Biol 2007; 3:29 - 35; http://dx.doi.org/10.1038/nchembio847; PMID: 17173027
   PubMed Web of Science ®Google Scholar
• Berkowitz SA, Engen JR, Mazzeo JR, Jones GB. Analytical tools for characterizing biopharmaceuticals and the implications for biosimilars. Nat Rev Drug Discov 2012; 11:527 - 40; http://dx.doi.org/10.1038/nrd3746; PMID: 22743980
   PubMed Web of Science ®Google Scholar
• Chirino AJ, Mire-Sluis A. Characterizing biological products and assessing comparability following manufacturing changes. Nat Biotechnol 2004; 22:1383 - 91; http://dx.doi.org/10.1038/nbt1030; PMID: 15529163
   PubMed Web of Science ®Google Scholar
• Queiroz JA, Tomaz CT, Cabral JM. Hydrophobic interaction chromatography of proteins. J Biotechnol 2001; 87:143 - 59; http://dx.doi.org/10.1016/S0168-1656(01)00237-1; PMID: 11278038
   PubMed Web of Science ®Google Scholar
• Geng X, Wang L. Liquid chromatography of recombinant proteins and protein drugs. J Chromatogr B Analyt Technol Biomed Life Sci 2008; 866:133 - 53; http://dx.doi.org/10.1016/j.jchromb.2008.01.041; PMID: 18294930
   PubMed Web of Science ®Google Scholar
• Boyd D, Kaschak T, Yan B. HIC resolution of an IgG1 with an oxidized Trp in a complementarity determining region. J Chromatogr B Analyt Technol Biomed Life Sci 2011; 879:955 - 60; http://dx.doi.org/10.1016/j.jchromb.2011.03.006; PMID: 21440514
   PubMed Web of Science ®Google Scholar
• Valliere-Douglass J, Wallace A, Balland A. Separation of populations of antibody variants by fine tuning of hydrophobic-interaction chromatography operating conditions. J Chromatogr A 2008; 1214:81 - 9; http://dx.doi.org/10.1016/j.chroma.2008.10.078; PMID: 19012891
   PubMed Web of Science ®Google Scholar
• Valliere-Douglass J, Jones L, Shpektor D, Kodama P, Wallace A, Balland A, Bailey R, Zhang Y. Separation and characterization of an IgG2 antibody containing a cyclic imide in CDR1 of light chain by hydrophobic interaction chromatography and mass spectrometry. Anal Chem 2008; 80:3168 - 74; http://dx.doi.org/10.1021/ac702245c; PMID: 18355059
   PubMed Web of Science ®Google Scholar
• Valliere-Douglass JF, Brady LJ, Farnsworth C, Pace D, Balland A, Wallace A, Wang W, Treuheit MJ, Yan B. O-fucosylation of an antibody light chain: characterization of a modification occurring on an IgG1 molecule. Glycobiology 2009; 19:144 - 52; http://dx.doi.org/10.1093/glycob/cwn116; PMID: 18952827
   PubMed Web of Science ®Google Scholar
• US patent Enbrel 7,294,481 B1.
   Google Scholar
• Ouellette D, Chumsae C, Clabbers A, Radziejewski C, Correia I. Comparison of the in vitro and in vivo stability of a succinimide intermediate observed on a therapeutic IgG1 molecule. MAbs 2013; 5:432 - 44; http://dx.doi.org/10.4161/mabs.24458; PMID: 23608772
   PubMed Web of Science ®Google Scholar
• Wakankar AA, Borchardt RT, Eigenbrot C, Shia S, Wang YJ, Shire SJ, Liu JL. Aspartate isomerization in the complementarity-determining regions of two closely related monoclonal antibodies. Biochemistry 2007; 46:1534 - 44; http://dx.doi.org/10.1021/bi061500t; PMID: 17279618
   PubMed Web of Science ®Google Scholar
• Grebenau RC, Goldenberg DM, Chang CH, Koch GA, Gold DV, Kunz A, Hansen HJ. Microheterogeneity of a purified IgG1 due to asymmetric Fab glycosylation. Mol Immunol 1992; 29:751 - 8; http://dx.doi.org/10.1016/0161-5890(92)90185-Z; PMID: 1603094
   PubMed Web of Science ®Google Scholar
• Harris RJ. Heterogeneity of recombinant antibodies: linking structure to function. Dev Biol (Basel) 2005; 122:117 - 27; PMID: 16375256
   PubMedGoogle Scholar
• Inouye K, Morimoto K. Single-step purification of F(ab’)2 mu fragments of mouse monoclonal antibodies (immunoglobulins M) by hydrophobic interaction high-performance liquid chromatography using TSKgel ether-5PW. J Biochem Biophys Methods 1993; 26:27 - 39; http://dx.doi.org/10.1016/0165-022X(93)90019-K; PMID: 8482788
   PubMedGoogle Scholar
• Wakankar A, Chen Y, Gokarn Y, Jacobson FS. Analytical methods for physicochemical characterization of antibody drug conjugates. MAbs 2011; 3:161 - 72; http://dx.doi.org/10.4161/mabs.3.2.14960; PMID: 21441786
   PubMed Web of Science ®Google Scholar
• Scheich C, Leitner D, Sievert V, Leidert M, Schlegel B, Simon B, Letunic I, Büssow K, Diehl A. Fast identification of folded human protein domains expressed in E. coli suitable for structural analysis. BMC Struct Biol 2004; 4:4; http://dx.doi.org/10.1186/1472-6807-4-4; PMID: 15113422
   PubMedGoogle Scholar
• Alpert AJ. High performance hydrophobic interaction chromatography of proteins on a series of poly(alkyl aspartamide)-silicas. J Chromatogr A 1986; 359:85 - 97; http://dx.doi.org/10.1016/0021-9673(86)80064-4
   Web of Science ®Google Scholar
• Mohler KM, Torrance DS, Smith CA, Goodwin RG, Stremler KE, Fung VP, Madani H, Widmer MB. Soluble tumor necrosis factor (TNF) receptors are effective therapeutic agents in lethal endotoxemia and function simultaneously as both TNF carriers and TNF antagonists. J Immunol 1993; 151:1548 - 61; PMID: 8393046
   PubMed Web of Science ®Google Scholar
• Declerck PJ. Biosimilar monoclonal antibodies: a science-based regulatory challenge. Expert Opin Biol Ther 2013; 13:153 - 6; http://dx.doi.org/10.1517/14712598.2012.758710; PMID: 23286777
   PubMed Web of Science ®Google Scholar
• Du Y, Walsh A, Ehrick R, Xu W, May K, Liu H. Chromatographic analysis of the acidic and basic species of recombinant monoclonal antibodies. MAbs 2012; 4:578 - 85; http://dx.doi.org/10.4161/mabs.21328; PMID: 22820257
   PubMed Web of Science ®Google Scholar
• Teshima G, Li MX, Danishmand R, Obi C, To R, Huang C, Kung J, Lahidji V, Freeberg J, Thorner L, et al. Separation of oxidized variants of a monoclonal antibody by anion-exchange. J Chromatogr A 2011; 1218:2091 - 7; http://dx.doi.org/10.1016/j.chroma.2010.10.107; PMID: 21145555
   PubMed Web of Science ®Google Scholar
• Arakawa T, Tsumoto K, Nagase K, Ejima D. The effects of arginine on protein binding and elution in hydrophobic interaction and ion-exchange chromatography. Protein Expr Purif 2007; 54:110 - 6; http://dx.doi.org/10.1016/j.pep.2007.02.010; PMID: 17408966
   PubMed Web of Science ®Google Scholar
• Yang X, Xu W, Dukleska S, Benchaar S, Mengisen S, Antochshuk V, Cheung J, Mann L, Babadjanova Z, Rowand J, et al. Developability studies before initiation of process development: improving manufacturability of monoclonal antibodies. MAbs 2013; 5:787 - 94; http://dx.doi.org/10.4161/mabs.25269; PMID: 23883920
   PubMed Web of Science ®Google Scholar
• Robinson NE, Robinson AB. in Molecular Clocks: Deamidation of Asparaginyl and Glutaminyl Residues in Peptides and Proteins. Althouse Press, Cave Junction, OR (2004)
   Google Scholar
• Hermeling S, Crommelin DJ, Schellekens H, Jiskoot W. Structure-immunogenicity relationships of therapeutic proteins. Pharm Res 2004; 21:897 - 903; http://dx.doi.org/10.1023/B:PHAM.0000029275.41323.a6; PMID: 15212151
   PubMed Web of Science ®Google Scholar
• Kumar V, Dixit N, Zhou LL, Fraunhofer W. Impact of short range hydrophobic interactions and long range electrostatic forces on the aggregation kinetics of a monoclonal antibody and a dual-variable domain immunoglobulin at low and high concentrations. Int J Pharm 2011; 421:82 - 93; http://dx.doi.org/10.1016/j.ijpharm.2011.09.017; PMID: 21959107
   PubMed Web of Science ®Google Scholar
• Joubert MK, Luo Q, Nashed-Samuel Y, Wypych J, Narhi LO. Classification and characterization of therapeutic antibody aggregates. J Biol Chem 2011; 286:25118 - 33; http://dx.doi.org/10.1074/jbc.M110.160457; PMID: 21454532
   PubMed Web of Science ®Google Scholar
• Chennamsetty N, Voynov V, Kayser V, Helk B, Trout BL. Design of therapeutic proteins with enhanced stability. Proc Natl Acad Sci U S A 2009; 106:11937 - 42; http://dx.doi.org/10.1073/pnas.0904191106; PMID: 19571001
   PubMed Web of Science ®Google Scholar
• Chennamsetty N, Helk B, Voynov V, Kayser V, Trout BL. Aggregation-prone motifs in human immunoglobulin G. J Mol Biol 2009; 391:404 - 13; http://dx.doi.org/10.1016/j.jmb.2009.06.028; PMID: 19527731
   PubMed Web of Science ®Google Scholar
• Perchiacca JM, Ladiwala AR, Bhattacharya M, Tessier PM. Aggregation-resistant domain antibodies engineered with charged mutations near the edges of the complementarity-determining regions. Protein Eng Des Sel 2012; 25:591 - 601; http://dx.doi.org/10.1093/protein/gzs042; PMID: 22843678
   PubMed Web of Science ®Google Scholar
• Wu SJ, Luo J, O’Neil KT, Kang J, Lacy ER, Canziani G, Baker A, Huang M, Tang QM, Raju TS, et al. Structure-based engineering of a monoclonal antibody for improved solubility. Protein Eng Des Sel 2010; 23:643 - 51; http://dx.doi.org/10.1093/protein/gzq037; PMID: 20543007
   PubMed Web of Science ®Google Scholar
• Lauer TM, Agrawal NJ, Chennamsetty N, Egodage K, Helk B, Trout BL. Developability index: a rapid in silico tool for the screening of antibody aggregation propensity. J Pharm Sci 2012; 101:102 - 15; http://dx.doi.org/10.1002/jps.22758; PMID: 21935950
   PubMed Web of Science ®Google Scholar
• Kayser V, Chennamsetty N, Voynov V, Helk B, Trout BL. Conformational stability and aggregation of therapeutic monoclonal antibodies studied with ANS and Thioflavin T binding. MAbs 2011; 3:408 - 11; http://dx.doi.org/10.4161/mabs.3.4.15677; PMID: 21540645
   PubMed Web of Science ®Google Scholar
• Rustandi R, Beck A, eds. Glycosylation Engineering of Biopharmaceuticals: Methods and Protocols, Methods in Molecular Biology, (2013) vol. 988.
   Google Scholar
• 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; http://dx.doi.org/10.1016/S0731-7085(97)00153-2; PMID: 9502154
   PubMed Web of Science ®Google Scholar
• Ambrogelly A, Antochshuk V, Shi S, Liu Z, Shameem M. A path to building quality during monoclonal antibody candidate selection in Monoclonal antibodies - development, delivery and applications. Future Science 2014; in the press
   Google Scholar
• Hamblett KJ, Senter PD, Chace DF, Sun MM, Lenox J, Cerveny CG, Kissler KM, Bernhardt SX, Kopcha AK, Zabinski RF, et al. Effects of drug loading on the antitumor activity of a monoclonal antibody drug conjugate. Clin Cancer Res 2004; 10:7063 - 70; http://dx.doi.org/10.1158/1078-0432.CCR-04-0789; PMID: 15501986
   PubMed Web of Science ®Google Scholar