Addressing new analytical challenges in protein formulation development

European Journal of Pharmaceutics and Biopharmaceutics

Volumn 78, Issue 2, 2011, Pages 196-207

  MacH, Henryk ^a   Arvinte, Tudor ^b,c  

^a MERCK RESEARCH LABORATORIES   (United States)

^b UNIVERSITY OF GENEVA   (Switzerland)

^c Therapeomic Inc   (Switzerland)

Author keywords

Analytical ultracentrifugation; Flow cytometry; Formulation; Phase separation; Spectroscopic methods; Therapeutic proteins

Indexed keywords

DNA; FLUORESCENT DYE; MONOCLONAL ANTIBODY;

ANTIGEN BINDING; ATOMIC FORCE MICROSCOPY; DIFFERENTIAL SCANNING CALORIMETRY; DNA DETERMINATION; DRUG BINDING; DRUG BIOAVAILABILITY; EX VIVO STUDY; FLOW CYTOMETRY; FLUORESCENCE SPECTROSCOPY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROPHOBICITY; MACROMOLECULE; MOLECULAR WEIGHT; NONHUMAN; PH; PHASE SEPARATION; POLYMERASE CHAIN REACTION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DETERMINATION; REVIEW; SUBCUTANEOUS TISSUE; TEMPERATURE; ULTRACENTRIFUGATION; ULTRAVIOLET SPECTROSCOPY; VISCOSITY;

EID: 79955799621     PISSN: 09396411     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejpb.2011.03.001     Document Type: Article

References (100)

1. G. Walsh, Biopharmaceuticals: recent approvals and likely directions, Trends Biotechnol. 23 (2005) 553-558. (Pubitemid 41483772)
2. H.-C. Mahler, W. Friess, U. Grauschopf, S. Kiese, Protein aggregation: pathways, induction factors and analysis, J. Pharm. Sci. 98 (2009) 2909-2934.
3. S.J. Shire, Z. Shahrokh, J. Liu, Challenges in the development of high protein concentration formulations, Biotechnol.: Pharm. Aspects 11 (2010) 131-147.
4. A. Saluja, D.S. Kalonia, Nature and consequences of protein-protein interactions in high protein concentration solutions, Int. J. Pharm. 358 (2008) 1-15.
5. C.-T. Huang, D. Sharma, P. Oma, R. Krishnamurthy, Quantitation of protein particles in parenteral solutions using micro-flow imaging, J. Pharm. Sci. 98 (2009) 3058-3071.
6. D. Griffiths, P. Hole, J. Smith, B. Carr, Characterization of nanoparticle dispersions by size, scattering intensity simultaneously, Nanotech Conf. Expo 1 (2009) 414-416.
7. V. Filipe, A. Hawe, W. Jiskoot, Critical evaluation of nanoparticle tracking analysis (NTA) by nanosight for the measurement of nanoparticles and protein aggregates, Pharm. Res. 27 (2010) 796-810.
8. J.P. Gabrielson, M.L. Brader, A.H. Pekar, K.B. Mathis, G. Winter, J.F. Carpenter, T.W. Randolph, Quantitation of aggregate levels in a recombinant humanized monoclonal antibody formulation by size-exclusion chromatography, asymmetrical flow field flow fractionation, and sedimentation velocity, J. Pharm. Sci. 96 (2006) 268-279. (Pubitemid 46363558)
9. B. Demeule, C. Palais, G. Machaidze, R. Gurny, T. Arvinte, New methods allowing the detection of protein aggregates: a case study on trastuzumab, MAbs 1 (2009) 142-150.
10. T. Arakawa, J.S. Philo, D. Ejima, H. Sato, K. Tsumoto, Aggregation analysis of therapeutic proteins, part 3: principles and optimization of field-flow fractionation (FFF), BioProcess Int. 5 (2007) 52. 54, 56, 58, 60-62, 64, 66, 68, 70.
11. K. Wuchner, J. Buechler, R. Spycher, P. Dalmonte, D.B. Volkin, Development of a microflow digital imaging assay to characterize protein particulates during storage of a high concentration IgG1 monoclonal antibody formulation, J. Pharm. Sci. 99 (2010) 3343-3361.
12. M.A.H. Capelle, R. Gurny, T. Arvinte, High throughput screening of protein formulation stability: practical considerations, Eur. J. Pharm. Biopharm. 65 (2007) 131-148. (Pubitemid 46038086)
13. M.A.H. Capelle, R. Gurny, T. Arvinte, High throughput methods to characterize protein permeation and release, Int. J. Pharm. 350 (2008) 272-278.
14. J.F. Carpenter, T.W. Randolph, W. Jiskoot, D.J.A. Crommelin, C.R. Middaugh, G. Winter, Y.-X. Fan, S. Kirshner, D. Verthelyi, S. Kozlowski, K.A. Clouse, P.G. Swann, A. Rosenberg, B. Cherney, Overlooking subvisible particles in therapeutic protein products: gaps that may compromise product quality, J. Pharm. Sci. 98 (2009) 1201-1205.
15. S.K. Singh, N. Afonina, M. Awwad, K. Bechtold-Peters, J.T. Blue, D. Chou, M. Cromwell, H.-J. Krause, H.-C. Mahler, B.K. Meyer, L. Narhi, D.P. Nesta, T. Spitznagel, An industry perspective on the monitoring of subvisible particles as a quality attribute for protein therapeutics, J. Pharm. Sci. 99 (2010) 3302-3321.
16. E.Y. Chi, S. Krishnan, T.W. Randolph, J.F. Carpenter, Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation, Pharm. Res. 20 (2003) 1325-1336.
17. T.W. Randolph, E.Y. Chi, S. Krishnan, B.S. Kendrick, J.F. Carpenter. Protein aggregation-conformational stability and colloidal stability, Abstracts of Papers, 224th ACS National Meeting, Boston, MA, United States, August 18-22, 2002 BIOT-160, 2002.
18. M.E.M. Cromwell, E. Hilario, F. Jacobson, Protein aggregation and bioprocessing, AAPS J. 8 (2006) E572-E579. (Pubitemid 44458092)
19. C.J. Roberts, Non-native protein aggregation kinetics, Biotechnol. Bioeng. 98 (2007) 927-938.
20. R. Jaenicke, Protein stability and protein folding, Ciba Found Symposium, vol. 161, pp. 206-216 (discussion pp. 217-221).
21. Y. Goto, L.J. Calciano, A.L. Fink, Acid-induced folding of proteins, Proc. Natl. Acad. Sci. USA 87 (1990) 573-577.
22. E. Vazquez-Contreras, P.I. Rodriguez, V. Castillo-Sanchez, M.E. Chanez- Cardenas, The unfolding of proteins induced by different denaturants, Adv. Protein Phys. Chem. (2008) 169-192.
23. J. Wallach, Stability studies of protein pharmaceuticals, Pharm. Ind. 71 (2009) 687-688. 690-692.
24. T. Wehr, R. Rodriquez-Diaz, Use of size exclusion chromatography in biopharmaceutical development, Analytical Techniques for Biopharmaceutical Development, Marcel Dekker, Inc., New York, NY, 2005. 95-112.
25. O.P. Sharma, D.K. Pollo, M.J. Sukumar, Quantification and characterization of subvisible proteinacious particles in opalescent mAb formulations using micro-flow imaging, J. Pharm. Sci. 99 (2010) 2628-2642.
26. M. Vujtek, R. Kubinek, R. Zboril, The role of atomic force microscopy in nanoparticle research, J. Adv. Microsc. Res. 5 (2010) 67-77.
27. A. Ikai, A review on: atomic force microscopy applied to nano-mechanics of the cell, Adv. Biochem. Eng./Biotechnol. 119 (2010) 47-61.
28. R. Creasey, S. Sharma, J.E. Craig, C.T. Gibson, A. Ebner, P. Hinterdorfer, N.H. Voelcker, Detecting protein aggregates on untreated human tissue samples by atomic force microscopy recognition imaging, Biophys. J. 99 (2010) 1660-1667.
29. K.J. Weronski, P. Cea, I. Diez-Perez, M.A. Busquets, J. Prat, V. Girona, Timelapse atomic force microscopy observations of the morphology, growth rate, and spontaneous alignment of nanofibers containing a peptide-amphiphile from the hepatitis G virus (NS3 protein), J. Phys. Chem. B 114 (2010) 620-625.
30. J.C. Johnson, S.R. Nettikadan, S.G. Vengasandra, E.J. Henderson, Analysis of solid-phase immobilized antibodies by atomic force microscopy, Biochem. Biophys. Methods 59 (2004) 167-180.
31. J. Legleiter, T. Kowalewski, Atomic force microscopy, Protein Rev. 4 (2006) 315-334.
32. T.J. Smith, Structural studies on antibody-virus complexes, Adv. Protein Chem. 64 (2003) 409-453.
33. N.H. Thomson, Imaging the substructure of antibodies with tapping-mode AFM in air: the importance of a water layer on mica, J. Microsc. (Oxford, UK) 217 (2005) 193-199.
34. J.N. Lin, B. Drake, A.S. Lea, P.K. Hansma, J.D. Andrade, Direct observation of immunoglobulin adsorption dynamics using the atomic force microscope, Langmuir 6 (1990) 509-511. (Pubitemid 20663814)
35. H. Lee, M. Kirchmeier, H. Mach, Monoclonal antibody aggregation intermediates visualized by atomic force microscopy, J. Pharm. Sci. 100 (2011) 416-423.
36. A.H. Fradkin, J.F. Carpenter, T.W. Randolph, Immunogenicity of aggregates of recombinant human growth hormone in mouse models, J. Pharm. Sci. 98 (2009) 3247-3264.
37. H.M. Dintzis, R.Z. Dintzis, B. Vogelstein, Molecular determinants of immunogenicity: the immunon model of immune response, Proc. Natl. Acad. Sci. USA 73 (1976) 3671-3675.
38. A.S. Rosenberg, Effects of protein aggregates: an immunologic perspective, AAPS J. 8 (2006) E501-E507. (Pubitemid 44294011)
39. S. Hermeling, D.J.A. Crommelin, H. Schellekens, W. Jiskoot, Immunogenicity of therapeutic proteins, Handb. Pharm. Biotechnol. (2007) 815-833.
40. H. Schellekens, W. Jiskoot, Immunogenicity of therapeutic proteins, Pharm. Biotechnol., third ed., 2008, pp. 125-132.
41. W. Jiskoot, E.C. Beuvery, A.A.M. De Koning, J.N. Herron, D.J.A. Crommelin, Analytical approaches to the study of monoclonal antibody stability, Pharm. Res. 7 (1990) 1234-1241.
42. T. Arvinte, Analytical methods for protein formulations, in: W. Jiskootand, D.J.A. Crommelin (Eds.), Methods for Structural Analysis of Protein Pharmaceuticals, AAPS Press, Arlington, VA, 2005, pp. 661-666.
43. S.J. Shire, J.J. Liu, Development of high protein concentration pharmaceuticals for SC delivery: fitting all the pieces together, Abstracts of Papers, 239th ACS National Meeting, San Francisco, CA, United States, 2010, pp. BIOT-132.
44. S. Kanai, J. Liu, T.W. Patapoff, S.J. Shire, Reversible self-association of a concentrated monoclonal antibody solution mediated by Fab-Fab interaction that impacts solution viscosity, J. Pharm. Sci. 97 (2008) 4219-4227.
45. R.P. Haughland, Handbook of Fluorescence Probes and Research Products, Sixth ed., Molecular Probes, Eugene, OR, 1996.
46. B. Demeule, R. Gurny, T. Arvinte, Detection and characterization of protein aggregates by fluorescence microscopy, Int. J. Pharm. 329 (2007) 37-45.
47. A. Hawe, M. Sutter, W. Jiskoot, Extrinsic fluorescent dyes as tools for protein characterization, Pharm. Res. 25 (2008) 1487-1499.
48. W. Jiskoot, A. Hawe, Aggregates enlightened: fluorescent dyes for detecting protein aggregates, BIOforum Eur. 13 (2009) 26-27.
49. P. Greenspan, S.D. Fowler, Spectrofluorometric studies of the lipid probe, Nile Red, J. Lipid Res. 26 (1985) 781-789. (Pubitemid 15046441)
50. D.L. Sackett, J.R. Knutson, J. Wolff, Hydrophobic surfaces of tubulin probed by time-resolved and steady-state fluorescence of Nile Red, J. Biol. Chem. 265 (1990) 14899-14906.
51. H.H. Bauer, A.F. Drake, H.P. Merkle, T. Arvinte, Fluorescence study of human calcitonin fibrillation kinetics using the hydrophobic probe Nile Red, in: Peptides 1992, Proceedings of the 22nd European Peptide Symposium, 1993, pp. 505-506.
52. Y. Li, H. Mach, J.T. Blue, High-throughput screening of monoclonal antibody aggregation behaviors, Abstracts of Papers, 239th ACS National Meeting, San Francisco, CA, United States, March 21-25, 2010, BIOT-558, 2010.
53. A. Hawe, W. Friess, M. Sutter, W. Jiskoot, Online fluorescent dye detection method for the characterization of immunoglobulin G aggregation by size exclusion chromatography and asymmetrical flow field flow fractionation, Anal. Biochem. 378 (2008) 115-122.
54. M.A.H. Capelle, P. Brugger, T. Arvinte, Spectroscopic characterization of antibodies adsorbed to aluminium adjuvants: correlation with antibody vaccine immunogenicity, Vaccine 23 (2005) 1686-1694. (Pubitemid 40215702)
55. B. Demeule, R. Gurny, T. Arvinte, Detection, characterization of protein aggregates by fluorescence microscopy, Int. J. Pharm. 329 (2007) 37-45. (Pubitemid 44937520)
56. A. Supersaxo, W.R. Hein, H. Steffen, Effect of molecular weight on the lymphatic absorption of water-soluble compounds following subcutaneous administration, Pharm. Res. 7 (1990) 167-169.
57. S.A. Charman, A.M. Segrave, G.A. Edwards, C.J. Porter, Systemic availability, lymphatic transport of human growth hormone administered by subcutaneous injection, J. Pharm. Sci. 89 (2005) 168-177. (Pubitemid 30120797)
58. C.J. Porter, S.A. Charman, Lymphatic transport of proteins after subcutaneous administration, J. Pharm. Sci. 89 (2009) 297-310.
59. J. Brange, D.R. Owens, S. Kang, A. Volund, Monomeric insulins, their experimental, clinical implications, Diabetes Care 13 (1990) 23-54.
60. E. Fernqvist, B. Linde, J. Ostman, R. Gunnarsson, Effects of physical exercise on insulin absorption in insulin-dependent diabetics. A comparison between human and porcine insulin, Clin. Physiol. 6 (1986) 489-497.
61. B. Linde, Dissociation of insulin absorption and blood flow during massage of a subcutaneous injection site, Diabetes Care 9 (1986) 570-574. (Pubitemid 17208934)
62. H. Mach, S. Gregory, S. Mittal, A. Lalloo, M. Kirchmeier, M. Shameem, Electrostatic interactions of monoclonal antibodies with subcutaneous tissue, Ther. Deliv., in press.
63. T. Ahamed, B.K. Nfor, P.D.E.M. Verhaert, G.W.K. Van Dedem, L.A.M. van der Wielen, M.H.M. Eppink, E.J.A.X. van de Sandt, M. Ottens, pH-gradient ion-exchange chromatography: an analytical tool for design and optimization of protein separations, J. Chromatogr. A 1164 (2007) 181-188. (Pubitemid 47284107)
64. D. Daitoku, T. Kurose, E. Mori, M. Hashimoto, S. Kawamata, Changes in the rat subcutaneous connective tissue after saline and histamine injection in relation to fluid storage and excretion, Arch. Histol. Cytol. 70 (2007) 29-41. (Pubitemid 46917491)
65. L.H. Bookbinder, A. Hofer, M.F. Haller, M.L. Zepeda, G.A. Keller, J.E. Lim, T.S. Edgington, H.M. Shepard, J.S. Patton, G.I. Frost, A recombinant human enzyme for enhanced interstitial transport of therapeutics, J. Controlled Release 114 (2006) 230-241. (Pubitemid 44291844)
66. XolairR, Prescribing information, www.xolair.com/prescribing-information. html.
67. T.A. Waldmann, W. Strober, Metabolism of immunoglobulins, Progr. Allergy 13 (1969) 1-110.
68. W.E. Wang, J.P. Balthasar, Monoclonal antibody pharmacokinetics and pharmacodynamics, Clin. Pharm. Ther. 84 (2008) 548-558.
69. R.P. Junghans, Finally! The Brambell receptor (FcRB). Mediator of transmission of immunity and protection from catabolism for IgG, Immunol. Res. 16 (1997) 29-57.
70. H. Mach, C.R. Middaugh, R.V. Lewis, Statistical determination of the average values of the extinction coefficients of tryptophan, tyrosine in native proteins, Anal. Biochem. 200 (1992) 74-80.
71. C.N. Pace, F. Vajdos, L. Fee, G. Grimsley, T. Gray, How to measure, predict the molar absorption coefficient of a protein, Protein Sci. 4 (1995) 2411-2423.
72. H. Mach, C.R. Middaugh, Ultraviolet spectroscopy as a tool in therapeutic protein development, J. Pharm. Sci. 100 (2011) 1214-1227.
73. I. Oreskes, D. Mandel, Spectrophotometric assay with turbidity correction of sized immunoglobulin G aggregates, Anal. Biochem. 99 (1979) 346-351.
74. A.F. Winder, W.L.G. Gent, Correction of light-scattering errors in spectrophotometric protein determinations, Biopolymers 10 (1971) 1243-1251.
75. A. Bootz, V. Vogel, D. Schubert, J. Kreuter, Comparison of scanning electron microscopy, dynamic light scattering and analytical ultracentrifugation for the sizing of poly(butyl cyanoacrylate) nanoparticles, Eur. J. Pharm. Biopharm. 57 (2004) 369-375.
76. H. Mach, A. Bhambhani, B.K. Meyer, S. Burek, H. Davis, J.T. Blue, R.K. Evans, The use of flow cytometry for the detection of therapeutic protein aggregates, J. Pharm. Sci. 100 (2011) 1671-1678.
77. D.B. Ludwig, J.T. Trotter, J.P. Gabrielson, J.F. Carpenter, T.W. Randolph, Flow cytometry: a promising technique for the study of silicone oil-induced particulate formation in protein formulations, Anal. Biochem. 410 (2011) 191-199.
78. F. He, D.H. Phan, S. Hogan, R. Bailey, G.W. Becker, L.O. Narhi, V.I. Razinkov, Detection of IgG aggregation by a high throughput method based on extrinsic fluorescence, J. Pharm. Sci. 99 (2010) 2598-2608.
79. F. He, S. Hogan, R.F. Latypov, L.O. Narhi, V.I. Razinkov, High throughput thermostability screening of monoclonal antibody formulations, J. Pharm. Sci. 99 (2010) 1707-1720.
80. M.D. Cummings, M.A. Farnum, M.I. Nelen, Universal screening methods, applications of thermofluor, J. Biomol. Screen. 1 (2006) 854-863. (Pubitemid 44562327)
81. U.B. Ericsson, B.M. Hallberg, G.T. DeTitta, N. Dekker, P. Nordlund, Thermofluor-based high-throughput stability optimization of proteins for structural studies, Anal. Biochem. 357 (2006) 289-298.
82. M.E.M. Cromwell, J.F. Carpenter, T. Scherer, T.W. Randolph, Opalescence in antibody formulations is a solution critical phenomenon, Abstracts of Papers, 236th ACS National Meeting, Philadelphia, PA, United States, BIOT-029, 2008.
83. N. Taschner, S.A. Mueller, V.R. Alumalla, K.N. Goldie, A.F. Drake, U. Aebi, T. Arvinte, Modulation of antigenicity related to changes in antibody flexibility upon lyophilization [erratum to document cited in CA136:107411], J. Mol. Biol. 312 (2001) 579.
84. B.A. Salinas, H.A. Sathish, S.M. Bishop, N. Harn, J.F. Carpenter, T.W. Randolph, Understanding and modulating opalescence and viscosity in a monoclonal antibody formulation, J. Pharm. Sci. 99 (2009) 82-93.
85. H. Zimmer, Viscosity and viscosity measurements, Allgem. Osterr. Chem. U. Tech.-Ztg. 50 (1932) 47-50.
86. U. Teipel, A.C. Hordijk, U. Foerter-Barth, D.M. Hoffman, C. Huebner, V. Valtsifer, K.E. Newman, Rheology, Energ. Mater. (2005) 433-508.
87. P.T. Reardon, A.L. Graham, S. Feng, V. Chawla, R.S. Admuthe, L.A. Mondy, Non- Newtonian end effects in falling ball viscometry of concentrated suspensions, Rheol. Acta 46 (2007) 413-424. (Pubitemid 44896716)
88. F. He, G.W. Becker, J.R. Litowski, L.O. Narhi, D.N. Brems, V.I. Razinkov, High-throughput dynamic light scattering method for measuring viscosity of concentrated protein solutions, Anal. Biochem. 399 (2010) 141-143.
89. S.P. Sutera, R. Skalak, The history of Poiseuille's law, Annu. Rev. Fluid Mech. 25 (1993) 1-19.
90. N.-S. Chang, Formula for the viscosity of a glycerol-water mixture, Ind. Eng. Chem. Res. 47 (2008) 3285-3288.
91. M.S. Runge, T.M. Laue, D.A. Yphantis, M.R. Lifsics, A. Saito, M. Altin, K. Reinke, R.C. Williams Jr., ATP-induced formation of an associated complex between microtubules and neurofilaments, Proc. Natl. Acad. Sci. USA 78 (1981) 1431-1435.
92. W. Machtle, High-resolution, submicron particle size distribution analysis using gravitational-sweep sedimentation, Biophys. J. 76 (1999) 1080-1091.
93. H. Mach, D.B. Volkin, R.D. Troutman, B. Wang, Z. Luo, K.U. Jansen, L. Shi, Disassembly and reassembly of yeast-derived recombinant human papillomavirus virus-like particles (HPV VLPs), J. Pharm. Sci. 95 (2006) 2195-2206. (Pubitemid 44568530)
94. W.F. Stafford, E.H. Braswell, Sedimentation velocity multi-speed method for analyzing polydisperse solutions, Biophys. Chem. 108 (2004) 273-279.
95. B. Demeule, M.J. Lawrence, A.F. Drake, R. Gurny, T. Arvinte, Characterization of protein aggregation: the case of a therapeutic immunoglobulin, Biochim. Biophys. Acta-Proteins and Proteomics 1774 (2007) 146-153.
96. J.F. Carpenter, T.W. Randolph, W. Jiskoot, D.J.A. Crommelin, C.R. Middaugh, G. Winter, Potential inaccurate quantitation and sizing of protein aggregates by size exclusion chromatography: essential need to use orthogonal methods to assure the quality of therapeutic protein products, J. Pharm. Sci. 99 (2010) 2200-2208.
97. B. Demeule, S.J. Shire, J. Liu, Challenges in protein formulation: sub-visible particles characterization, Abstracts of Papers, 239th ACS National Meeting, San Francisco, CA, United States, March 21-25, BIOT-136, 2010.
98. T. Arvinte, Formulation of protein drugs - important points to consider, BioWorld Eur. 01 (2007) 6-9.
99. J.S. Philo, Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques, Anal. Biochem. 354 (2006) 238-246.
100. J.S. Philo, Analytical ultracentrifugation, Biotechnol.: Pharm. Aspects 3 (2005) 379-412.