A critical evaluation of self-interaction chromatography as a predictive tool for the assessment of protein-protein interactions in protein formulation development: A case study of a therapeutic monoclonal antibody

European Journal of Pharmaceutics and Biopharmaceutics

Volumn 75, Issue 1, 2010, Pages 16-25

  Le Brun, Virginie ^a   Friess, Wolfgang ^a   Bassarab, Stefan ^b   Mühlau, Silke ^b   Garidel, Patrick ^b  

^a UNIVERSITY OF MUNICH   (Germany)

^b BOEHRINGER INGELHEIM PHARMA GMBH AND CO KG   (Germany)

Author keywords

Antibody; B22; Colloidal stability; Immunoglobulin; Osmotic second virial coefficient; Protein interactions; Self interaction chromatography

Indexed keywords

IMMUNOGLOBULIN G1 ANTIBODY;

ANALYTICAL PARAMETERS; ARTICLE; CHEMICAL COMPOSITION; CHROMATOGRAPHY; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DRUG SCREENING; DRUG STABILITY; EXCIPIENT COMPATIBILITY; INFRARED SPECTROSCOPY; LIGHT SCATTERING; PROTEIN AGGREGATION; PROTEIN PROTEIN INTERACTION; PROTON TRANSPORT; SELF INTERACTION CHROMATOGRAPHY; TURBIDITY;

ANTIBODIES, MONOCLONAL; CHEMISTRY, PHARMACEUTICAL; CHROMATOGRAPHY, GEL; DRUG DISCOVERY; DRUG EVALUATION, PRECLINICAL; HUMANS; PREDICTIVE VALUE OF TESTS; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TECHNOLOGY, PHARMACEUTICAL;

EID: 77951652786     PISSN: 09396411     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejpb.2010.01.009     Document Type: Article

References (82)

1. Shire S.J., Shahrokh Z., Liu J. Challenges in the development of high protein concentration formulations. J. Pharm. Sci. 2004, 93(6):1390-1402.
2. Wang W., Singh S., Zeng D.L., King K., Nema S. Antibody structure, instability, and formulation. J. Pharm. Sci. 2007, 96(1):1-26.
3. 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(9):1325-1336.
4. Baynes B.M., Trout B.L. Rational design of solution additives for the prevention of protein aggregation. Biophys. J. 2004, 87:1631-1639.
5. Broglia R.A., Tiana G., Pasquali S., Roman H.E., Vigezzi E. Folding and aggregation of designed proteins. Proc. Natl. Acad. Sci. USA 1998, 95:12930-12933.
6. Dudgeon K., Famm K., Christ D. Sequence determinants of protein aggregation in human VH domains. Protein Eng. 2009, 22(3):217-220.
7. Trovato A., Senol F., Tosatto S.C.E. The PASTA server for protein aggregation prediction. Protein Eng. 2007, 20(10):521-523.
8. Harn N., Allan C., Oliver C., Middaugh C.R. Highly concentrated monoclonal antibody solutions: direct analysis of physical structure and thermal stability. J. Pharm. Sci. 2007, 96(3):532-546.
9. Garidel P., Schott H. Fourier-transform midinfrared spectroscopy for analysis and screening of liquid protein formulations. Part 2: detailed analysis and applications. BioProcess Int. 2006, 4:48-55.
10. Alford J.R., Kwok S.C., Roberts J.N., Wuttke D.S., Kendrick B.S., Carpenter J.F., Randolph T.W. High concentration formulations of recombinant human interleukin-1 receptor antagonist: I. Physical characterization. J. Pharm. Sci. 2008, 97(8):3035-3050.
11. Saluja A., Badkar A.V., Zeng D.L., Nema S., Kalonia D.S. Ultrasonic storage modulus as a novel parameter for analyzing protein-protein interactions in high protein concentration solutions: correlation with static and dynamic light scattering measurements. Biophys. J. 2007, 92(1):234-244.
12. Jimenez M., Rivas G., Minton A.P. Quantitative characterization of weak self-association in concentrated solutions of immunoglobulin G via the measurement of sedimentation equilibrium and osmotic pressure. Biochemistry 2007, 46(28):8373-8378.
13. Haynes C.A., Tamura K., Korfer H.R., Blanch H.W., Prausnitz J.M. Thermodynamic properties of aqueous alpha-chymotrypsin solutions from membrane osmometry measurements. J. Phys. Chem. 1992, 96(2):905-912.
14. Bajaj H., Sharma V.K., Kalonia D.S. Determination of second virial coefficient of proteins using a dual-detector cell for simultaneous measurement of scattered light intensity and concentration in SEC-HPLC. Biophys. J. 2004, 87:4048-4055.
15. Deszczynski M., Harding S.E., Winzor D.J. Negative second virial coefficients as predictors of protein crystal growth: evidence from sedimentation equilibrium studies that refutes the designation of those light scattering parameters as osmotic virial coefficients. Biophys. Chem. 2006, 120:106-113.
16. Tessier P.M., Sandler S.I., Lenhoff A.M. Direct measurement of protein osmotic second virial cross coefficients by cross-interaction chromatography. Protein Sci. 2004, 13:1379-1390.
17. Winzor D.J., Deszczynski M., Harding S.E., Wills P.R. Nonequivalence of second virial coefficients from sedimentation equilibrium and static light scattering studies of protein solutions. Biophys. Chem. 2007, 128:46-55.
18. Winzor D.J., Scott D.J., Wills P.R. A simpler analysis for the measurement of second virial coefficients by self-interaction chromatography. Anal. Biochem. 2007, 371:21-25.
19. Lebowitz J., Lewis M.S., Schuck P. Modern analytical ultracentrifugation in protein science: A tutorial review. Protein Sci. 2002, 11:2067-2079.
20. Minton A.P. Alternative strategies for the characterization of associations in multicomponent solutions via measurement of sedimentation equilibrium. Prog. Colloid Polym. Sci. 1997, 107:11-19.
21. Minton A.P. Quantitative characterization of reversible macromolecular associations via sedimentation equilibrium: an introduction. Exp. Mol. Med. 2000, 32:1-5.
22. Beeckmans S. Chromatographic methods to study protein-protein interactions. Methods 1999, 19:278-305.
23. Bloustine J., Berejnov V., Fraden S. Measurements of protein-protein interactions by size-exclusion chromatography. Biophys. J. 2003, 85:1619-1632.
24. Hahn R., Amatschek K., Schallaun E., Necina R. Performance of affinity chromatography with peptide ligands: influence of spacer, matrix composition and immobilization chemistry. Int. J. Bio-Chromatogr. 2000, 5(3):175-185.
25. Heftmann E. Chromatography: Fundamentals and Applications of Chromatography and Related Differential Migration Methods: Applications 2004, Elsevier.
26. Lemque R., Jaulmes A., Sebile B., Vidal-Madjar C. Study of the adsorption of self-associating proteins on an anion exchanger: application to the chromatography of β-lactoglobulin B. J. Chromatogr. 1992, 599:255-265.
27. Stevens F.J. Analysis of protein-protein interaction by simulation of small-zone size-exclusion chromatography: application to an antibody-antigen association. Biochemistry 1986, 25(5):981-993.
28. Wen J., Arakawa T., Philo J.S. Size-exclusion chromatography with on-line light scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal. Biochem. 1996, 240:155-166.
29. Winzor D.J. The development of chromatography for the characterization of protein interactions: a personal perspective. Biochem. Soc. Trans. 2003, 31(5):1010-1014.
30. Patro S.Y., Przybycien T.M. Self-interaction chromatography: a tool for the study of protein-protein interactions in bioprocessing environments. Biotechnol. Bioeng. 1996, 52:193-203.
31. Przybycien T.M. Protein-protein interactions as a means of purification. Curr. Opin. Biotechnol. 1998, 9:164-170.
32. Tessier P.M., Vandrey S.D., Berger B.W., Pazhianur R., Sandler S.I., Lenhoff A.M. Self-interaction chromatography: a novel screening method for rational protein crystallization. Acta Crystallogr. D: Biol. Crystallogr. 2002, 58:1531-1535.
33. Bonnete F., Finet S., Tardieu A. Second virial coefficient: variations with lysozyme crystallization conditions. J. Cryst. Growth 1999, 196(2-4):403-414.
34. Liu W., Bratko D., Prausnitz J.M., Blanch H.W. Effect of alcohols on aqueous lysozyme-lysozyme interactions from static light-scattering measurements. Biophys. Chem. 2004, 107(3):289-298.
35. Neal B.L., Asthagiri D., Velev O.D., Lenhoff A.M. Why is the osmotic second virial coefficient related to protein crystallization?. J. Cryst. Growth 1999, 196:377-387.
36. Johnson D.H., Parupudi A., Wilson W.W., Delucas L.J. High-throughput self-interaction chromatography: applications in protein formulation prediction. Pharm. Res. 2009, 26(2):269-305.
37. Tessier P.M., Lenhoff A.M., Sandler S.I. Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography. Biophys. J. 2002, 82(3):1620-1631.
38. Tessier P.M., Johnson H.R., Pazhianur R., Berger B.W. Predictive crystallization of ribonuclease A via rapid screening of osmotic second virial coefficients. Proteins 2003, 50:303-311.
39. Ahamed T., Esteban B.N.A., Ottens M., van Dedem G.W.K., van der Wielen L.A.M., Bisschops M.A.T., Lee A., Pham C., Thommes J. Phase behavior of an intact monoclonal antibody. Biophys. J. 2007, 93(2):610-619.
40. Liu J., Nguyen M.D., Andya J.D., Shire S.J. Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution. J. Pharm. Sci. 2005, 94(9):1928-1940.
41. Katayama D.S., Nayar R., Chou D.K., Valente J.J., Cooper J., Henry C.S., Vander Velde D.G., Villarete L., Liu C.P., Manning M.C. Effect of buffer species on the thermally induced aggregation of interferon-tau. J. Pharm. Sci. 2006, 95(6):1212-1226.
42. Bajaj H., Sharma V.K., Badkar A., Zeng D., Nema S., Kalonia D.S. Protein structural conformation and not second virial coefficient relates to long-term irreversible aggregation of a monoclonal antibody and ovalbumin in solution. Pharm. Res. 2006, 23(6):1382-1394.
43. Chi E.Y., Krishnan S., Kendrick B.S., Chang B.S., Carpenter J.F., Randolph T.W. Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Protein Sci. 2003, 12(5):903-913.
44. Alford J.R., Kendrick B.S., Carpenter J.F., Randolph T.W. Measurement of the second osmotic virial coefficient for protein solutions exhibiting monomer-dimer equilibrium. Anal. Biochem. 2008, 377(2):128-133.
45. Haas C., Drenth J., Wilson W.W. Relation between the solubility of proteins in aqueous solutions and the second virial coefficient of the solution. J. Phys. Chem. B 1999, 103(14):2808-2811.
46. Le Brun V., Friess W., Schultz-Fademrecht T., Muehlau S., Garidel P. Lysozyme-lysozyme self-interactions as assessed by the osmotic second virial coefficient: impact for physical protein stabilisation. Biotechnol. J. 2009, 4(9):1305-1319.
47. Lima E.R.A., Biscaia E.C., Bostrom M., Tavares F.W. Osmotic second virial coefficients and phase diagrams for aqueous proteins from a much-improved Poisson-Boltzmann equation. J. Phys. Chem. C 2007, 111:16055-16059.
48. Payne R.W., Nayar R., Tarantino R., Del Terzo S., Moschera J., Di J., Heilman D., Bray B., Manning M.C., Henry C.S. Second virial coefficient determination of a therapeutic peptide by self-interaction chromatography. Biopolymers 2006, 84(5):527-533.
49. Ruppert S., Sandler S.I., Lenhoff A.M. Correlation between the osmotic second virial coefficient and the solubility of proteins. Biotechnol. Prog. 2001, 17(1):182-187.
50. Stigter D., Hill T.L. Theory of the Donnan membrane equilibrium 2. Calculation of the osmotic pressure and of the salt distribution in a Donnan system with highly charged colloid particles. J. Phys. Chem. 1959, 63:551-556.
51. Wanka J., Peukert W. Die Bedeutung des zweiten osmotischen Virialkoeffizienten für die Proteinkristallization. Chem. Ing. Tech. 2008, 2996:273-278.
52. Garidel P., Schott H. Fourier-transform midinfrared spectroscopy for analysis and screening of liquid protein formulations. Part 1: understanding infrared spectroscopy of proteins. BioProcess Int. 2006, 4(5):40-46.
53. Tessier P.M., Lenhoff A.M. Measurements of protein self-association as a guide to crystallization. Curr. Opin. Biotechnol. 2003, 14:512-516.
54. Valente J.J., Payne R.W., Manning M.C., Wilson W.W., Henry C.S. Colloidal behavior of proteins: effects of the second virial coefficient on solubility, crystallization and aggregation of proteins in aqueous solution. Curr. Pharm. Biotechnol. 2005, 6(6):427-436.
55. Valente J.J., Verma K.S., Manning M.C., Wilson W.W., Henry C.S. Second virial coefficient studies of cosolvent-induced protein self-interaction. Biophys. J. 2005, 89:4211-4218.
56. Velev O.D., Kaler E.W., Lenhoff A.M. Protein interactions in solution characterized by light and neutron scattering: comparison of lysozyme and chymotrypsinogen. Biophys. J. 1998, 75:2682-2697.
57. Rice P., Longden I., Bleasby A. EMBOSS: the European molecular biology open software suite. Trends Genet. 2000, 16(6):276-277.
58. Mahler H.C., Muller R., Friess W., Delille A., Matheus S. Induction and analysis of aggregates in a liquid IgG1-antibody formulation. Eur. J. Pharm. Biopharm. 2005, 59(3):407-417.
59. Le Brun V., Friess W., Bassarab S., Garidel P. Correlation of protein-protein interactions as assessed by affinity chromatography with colloidal stability: a case study with lysozyme. Pharm. Dev. Technol. 2010, 10.1080/10837450903262074.
60. Bandekar J. Amide modes and protein conformation. Biochim. Biophys. Acta 1992, 1120(2):123-143.
61. Byler D.M., Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 1986, 25(3):469-487.
62. Dong A.C., Kendrick B., Kreilgard L., Matsuura J., Manning M.C., Carpenter J.F. Spectroscopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution. Arch. Biochem. Biophys. 1997, 347(2):213-220.
63. van de Weert M., Haris P.I., Hennink W.E., Crommelin D.J.A. Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors. Anal. Biochem. 2001, 297(2):160-169.
64. Hoffmann C., Blume A., Miller I., Garidel P. Insights into protein-polysorbate interactions analysed by means of isothermal titration and differential scanning calorimetry. Eur. Biophys. J. 2009, 38(5):557-568.
65. 2O. J. Cryst. Growth 1997, 178(4):575-584.
66. 2O solutions: a simple relationship. J. Cryst. Growth 1997, 177:238-247.
67. Piazza R. Protein interactions and association: an open challenge for colloid science. Curr. Opin. Colloid Interface Sci. 2004, 8(6):515-522.
68. Dill K.A. Dominant forces in protein folding. Biochemistry 1990, 29(31):7133-7155.
69. Shaw K.L., Grimsley G.R., Yakovlev G.I., Makarov A.A., Pace C.N. The effect of net charge on the solubility, activity, and stability of ribonuclease Sa. Protein Sci. 2001, 10(6):1206-1215.
70. Wang N., Hu B., Ionescu R., Mach H., Sweeney J., Hamm C., Kirchmeier M.J., Meyer B.K. Opalescence of an IgG1 monoclonal antibody formulation is mediated by ionic strength and excipients. BioPharm. Int. 2009, 22:36-47.
71. Saluja A., Kalonia D.S. Nature and consequences of protein-protein interactions in high protein concentration solutions. Int. J. Pharm. 2008, 358(1-2):1-15.
72. Arakawa T., Tsumoto K., Kita Y., Chang B., Ejima D. Biotechnology applications of amino acids in protein purification and formulations. Amino Acids 2007, 33(4):587-605.
73. Arakawa T., Ejima D., Tsumoto K., Obeyama N., Tanaka Y., Kita Y., Timasheff S.N. Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects. Biophys. Chem. 2007, 127(1-2):1-8.
74. Shiraki K., Kudou M., Fujiwara S., Imanaka T., Takagi M. Biophysical effect of amino acids on the prevention of protein aggregation. J. Biochem. 2002, 132(4):591-595.
75. Arakawa T., Philo J.S., Kita Y. Kinetic and thermodynamic analysis of thermal unfolding of recombinant erythropoietin. Biosci. Biotechnol. Biochem. 2001, 65(6):1321-1327.
76. Bummer P.M. Chemical considerations in protein and peptide stability. Drugs Pharm. Sci. 2008, 175:7-42.
77. Reubsaet J.L., Beijnen J.H., Bult A., van Maanen R.J., Marchal J.A., Underberg W.J. Analytical techniques used to study the degradation of proteins and peptides: chemical instability. J. Pharm. Biomed. Anal. 1998, 17(6-7):955-978.
78. Chen B., Bautista R., Yu K., Zapata G.A., Mulkerrin M.G., Chamow S.M. Influence of histidine on the stability and physical properties of a fully human antibody in aqueous and solid forms. Pharm. Res. 2003, 20(12):1952-1960.
79. Matheus S., Mahler H.C., Friess W. A critical evaluation of Tm (FTIR) measurements of high-concentration IgG(1) antibody formulations as a formulation development tool. Pharm. Res. 2006, 23(7):1617-1627.
80. Ionescu R.M., Vlasak J., Price C., Kirchmeier M. Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies. J. Pharm. Sci. 2008, 97(4):1414-1426.
81. Narhi L.O., Philo J.S., Sun B., Chang B.S., Arakawa T. Reversibility of heat-induced denaturation of the recombinant human megakaryocyte growth and development factor. Pharm. Res. 1999, 16(6):799-807.
82. Gokarn Y.R., Kras E., Nodgaard C., Dharmavaram V., Fesinmeyer R.M., Hultgen H., Brych S., Remmele R.L., Brems D.N., Hershenson S. Self-buffering antibody formulations. J. Pharm. Sci. 2008, 97(8):3051-3066.