Method development for the separation of monoclonal antibody charge variants in cation exchange chromatography, Part II: PH gradient approach

Journal of Pharmaceutical and Biomedical Analysis

Volumn 102, Issue , 2015, Pages 282-289

  Fekete, Szabolcs ^a   Beck, Alain ^b   Fekete, Jeno ^c   Guillarme, Davy ^a  

^a UNIVERSITY OF GENEVA   (Switzerland)

^b Centre d'Immunologie Pierre Fabre   (France)

^c BUDAPEST UNIVERSITY OF TECHNOLOGY AND ECONOMICS   (Hungary)

Author keywords

Cetuximab; Ion exchange; Method development; Monoclonal antibody; PH gradient

Indexed keywords

ADALIMUMAB; BEVACIZUMAB; CETUXIMAB; DENOSUMAB; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN FC FRAGMENT; MONOCLONAL ANTIBODY; NATALIZUMAB; OFATUMUMAB; PALIVIZUMAB; PANITUMUMAB; RITUXIMAB; SODIUM CHLORIDE; TRASTUZUMAB;

ARTICLE; CATION EXCHANGE; COMPARATIVE STUDY; DRUG ISOLATION; ELUTION; ION EXCHANGE CHROMATOGRAPHY; PH; SEPARATION TECHNIQUE; CHEMISTRY; ISOLATION AND PURIFICATION; PROCEDURES;

ANTIBODIES, MONOCLONAL; CHROMATOGRAPHY, ION EXCHANGE; HYDROGEN-ION CONCENTRATION;

EID: 84908391606     PISSN: 07317085     EISSN: 1873264X     Source Type: Journal    
DOI: 10.1016/j.jpba.2014.09.032     Document Type: Article

References (35)

1. Beck A., Cianferani S.S., Van Dorsselaer A. Biosimilar, biobetter, and next generation antibody characterization by mass spectrometry. Anal. Chem. 2012, 84:4637-4646.
2. Zhang Z., Pan H., Chen X. Mass spectrometry for structural characterization of therapeutic antibodies. Mass Spectrom. Rev. 2009, 28:147-176.
3. Perkins M., Theiler R., Lunte S., Jeschke M. Determination of the origin of charge heterogeneity in a murine monoclonal antibody. Pharm. Res. 2000, 17:1110-1117.
4. Fekete S., Gassner A.L., Rudaz S., Schappler J., Guillarme D. Analytical strategies for the characterization of therapeutic monoclonal antibodies. Trends Anal. Chem. 2013, 42:74-83.
5. Moorhouse K.G., Nashabeh W., Deveney J., Bjork N.S., Mulkerrin M.G., Ryskamp T. Validation of an HPLC method for the analysis of the charge heterogeneity of the recombinant monoclonal antibody IDEC-C2B8 after papain digestion. J. Pharm. Biomed. Anal. 1997, 16:593.
6. Lau H., Pace D., Yan B., McGrath T., Smallwood S., Patel K., Park J., Park S.S., Latypov R.F. Investigation of degradation processes in IgG1 monoclonal antibodies by limited proteolysis coupled with weak cation-exchange HPLC. J. Chromatogr. B 2010, 878:868-876.
7. Teshima G., Li M.X., Danishmand R., Obi C., To R., Huang C., Kung J., Lahidji V., Freeberg J., Thorner L., Tomic M. Separation of oxidized variants of a monoclonal antibody by anion-exchange. J. Chromatogr. A 2011, 1218:2091-2097.
8. Farnan D., Moreno G.T. Multiproduct high-resolution monoclonal antibody charge variant separations by pH gradient ion-exchange chromatography. Anal. Chem. 2009, 81:8846-8857.
9. Sluyterman L.A.Æ., Elgersma O. Chromatofocusing: isoelectric focusing on ion exchange columns. I. General principles. J. Chromatogr. 1978, 150:17-30.
10. Sluyterman L.A.Æ., Wijdenes J. Chromatofocusing: isoelectric focusing on ion exchange columns II. Experimental verification. J. Chromatogr. 1978, 150:31-44.
11. Sluyterman L.A.Æ., Wijdenes J. Chromatofocusing: IV. Properties of an agarose polyethyleneimine ion exchanger and its suitability for protein separation. J. Chromatogr. 1981, 206:441-447.
12. Rozhkova A. Quantitative analysis of monoclonal antibodies by cation-exchange chromatofocusing. J. Chromatogr. A 2009, 1216:5989-5994.
13. Kang X., Frey D. High-performance cation-exchange chromatofocusing of proteins. J. Chromatogr. A 2003, 991:117-128.
14. Shan L., Anderson D.J. Effect of buffer concentration on gradient chromatofocusing performance separating proteins on a high-performance DEAE column. J. Chromatogr. A 2001, 909:191-205.
15. Shan L., Anderson D.J. Gradient chromatofocusing versatile pH gradient separation of proteins in ion-exchange HPLC: characterization studies. Anal. Chem. 2002, 74:5641-5649.
16. Talebi M., Nordbog A., Gaspar A., Lacher N.A., Wang Q., He X.Z., Haddad P.R., Hilder E.F. Charge heterogeneity profiling of monoclonal antibodies using low ionic strength ion-exchange chromatography and well-controlled pH gradients on monolithic columns. J. Chromatogr. A 2013, 1317:148-154.
17. Ahamed T., Nfor B.K., Verhaert P.D.E.M., van Dedem G.W.K., van der Wielen L.A.M., Eppink M.H.M., van de Sandt E.J.A.X., Ottens M. pH-gradient ion-exchange chromatography: an analytical tool for design and optimization of protein separations. J. Chromatogr. A 2007, 1164:181-188.
18. Shan L., Anderson D.J. Gradient chromatofocusing. versatile pH gradient separation of proteins in ion-exchange HPLC: characterization studies. Anal. Chem. 2002, 74:5641-5649.
19. Liu Y., Anderson D.J. Gradient chromatofocusing high-performance liquid chromatography: I. Practical aspects. J. Chromatogr. A 1997, 762:207-217.
20. Rea J.C., Moreno G.T., Lou Y., Farnan D. Validation of a pH gradient based ion-exchange chromatography method for high-resolution monoclonal antibody charge variant separations. J. Pharm. Biomed. Anal. 2011, 54:317-323.
21. Zhang L., Patapoff T., Farnan D., Zhang B. Improving pH gradient cation-exchange chromatography of monoclonal antibodies by controlling ionic strength. J. Chromatogr. A 2013, 1272:56-64.
22. Fekete S., Rudaz S., Fekete J., Guillarme D. Analysis of recombinant monoclonal antibodies by RPLC: toward a generic method development approach. J. Pharm. Biomed. Anal. 2012, 70:158-168.
23. Fekete S., Fekete J., Molnár I., Ganzler K. Rapid high performance liquid chromatography method development with high prediction accuracy, using 5cm long narrow bore columns packed with sub-2μm particles and Design Space computer modeling. J. Chromatogr. A 2009, 1216:7816-7823.
24. Fekete S., Beck A., Fekete J., Guillarme D. Method development for the separation of monoclonal antibody charge variants in cation exchange chromatography, part I: salt gradient approach. J. Pharm. Biomed. Anal. 2014, 102C:33-44.
25. Ayoub D., Jabs W., Resemann A., Evers W., Evans C., Main L., Baessmann C., Wagner-Rousset E., Suckau D., Beck A. Correct primary structure assessment and extensive glyco-profiling of cetuximab by a combination of intact, middle-up, middle-down and bottom-up ESI and MALDI mass spectrometry techniques. mAbs 2013, 5:699-710.
26. Ishihara T., Yamamoto S. Optimization of monoclonal antibody purification by ion-exchange chromatography, application of simple methods with linear gradient elution experimental data. J. Chromatogr. A 2005, 1069:99-106.
27. Stout R.W., Sivakoff S.I., Ricker R.D., Snyder L.R. Separation of proteins by gradient elution from ion-exchange columns: optimizing experimental conditions. J. Chromatogr. 1986, 353:439-463.
28. Quarry M.A., Grob R.L., Snyder L.R. Prediction of precise isocratic retention data from two or more gradient elution runs. Analysis of some associated errors. Anal. Chem. 1986, 58:907-917.
29. Roth C.M., Unger K.K., Lenhoff A.M. Mechanistic model of retention in protein ion-exchange chromatography. J. Chromatogr. A 1996, 726:45-56.
30. Fekete S., Rudaz S., Veuthey J.L., Guillarme D. Impact of mobile phase temperature on recovery and stability of monoclonal antibodies using recent reversed phase stationary phases. J. Sep. Sci. 2012, 35:3113-3123.
31. Heinisch S., Rocca J.-L. Sense and non-sense of high-temperature liquid chromatography. J. Chromatogr. A 2009, 1216:642-658.
32. Chen Y., Mant C.T., Hodges R.S. Temperature selectivity effects in reversed-phase liquid chromatography due to conformation differences between helical and non-helical peptides. J. Chromatogr. A 2003, 1010:45-61.
33. Mant C.T., Chen Y., Hodges R.S. Temperature profiling of polypeptides in reversed-phase liquid chromatography: I. Monitoring of dimerization and unfolding of amphipathic α-helical peptides. J. Chromatogr. A 2003, 1009:29-43.
34. Mant C.T., Tripet B., Hodges R.S. Temperature profiling of polypeptides in reversed-phase liquid chromatography: II. Monitoring of folding and stability of two-stranded α-helical coiled-coils. J. Chromatogr. A 2003, 1009:45-59.
35. Neue U.D. Theory of peak capacity in gradient elution. J. Chromatogr. A 2005, 1079:153-161.