Accelerated stability studies of abatacept formulations: Comparison of freeze-thawing- and agitation-induced stresses

Journal of Pharmaceutical Sciences

Volumn 101, Issue 7, 2012, Pages 2307-2315

  Cordes, Amanda A ^a   Carpenter, John F ^b   Randolph, Theodore W ^a  

^a UCB 450   (United States)

^b UNIVERSITY OF COLORADO   (United States)

Author keywords

Agitation; Flow imaging; Freeze thaw; Fusion protein; Microparticles; Protein aggregation; Protein formulation; Proteins

Indexed keywords

ABATACEPT; ANTIBODY CONJUGATE; IMMUNOSUPPRESSIVE AGENT;

ACCELERATION; AGITATION; ARTICLE; BIOCHEMISTRY; COLLOID; CONTROLLED STUDY; DRUG CONFORMATION; DRUG FORMULATION; DRUG STABILITY; FREEZE THAWING; GEL PERMEATION CHROMATOGRAPHY; HIGH TEMPERATURE; INCUBATION TIME; IONIC STRENGTH; MECHANICAL STRESS; MICROFLOW IMAGING; MOLECULAR IMAGING; PH; PROTEIN AGGREGATION; ZETA POTENTIAL; CHEMISTRY; COMPARATIVE STUDY; FREEZING; GEL CHROMATOGRAPHY; PROTEIN CONFORMATION; PROTEIN STABILITY; TEMPERATURE;

CHROMATOGRAPHY, GEL; DRUG STABILITY; FREEZING; IMMUNOCONJUGATES; IMMUNOSUPPRESSIVE AGENTS; PROTEIN CONFORMATION; PROTEIN STABILITY; STRESS, MECHANICAL; TEMPERATURE;

EID: 84866280037     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23150     Document Type: Article

References (34)

1. Fast J, Cordes AA, Carpenter JF, Randolph TW. 2009. Physical instability of a therapeutic Fc fusion protein: Domain contributions to conformational and colloidal stability. Biochemistry 48:11724-11736.
2. Randolph TW, Carpenter JF. 2007. Engineering challenges of protein formulations. AIChE J 53:1902-1907.
3. Roberts CJ, Das TK, Sahin E. 2011. Predicting solution aggregation rates for therapeutic proteins: Approaches and challenges. Int J Pharm 418: 318-333.
4. Remmele RL, Zhank-van Enk J, Dharmavaram V, Balaban D, Durst M, Shoshitaishvili A, Rand H. 2005. Scan-rate dependent melting transitions of interleukin-1 receptor (type II): Elucidation of meaningful thermodynamic and kinetic parameters of aggregation acquired from DSC simulations. J Am Chem Soc 127:8328-8339.
5. Brummitt RK, Nesta DP, Roberts CJ. 2011. Predicting accelerated aggregation rates for monoclonal antibody formulations, and challenges for low-temperature predictions. J Pharm Sci [Epub ahead of print]. doi: 10.1002/jps.22633.
6. Cromwell M, Hilario E, Jacobson F. 2006. Protein aggregation and bioprocessing. AAPS J 8:572-579.
7. Rathore N, Rajan RS. 2008. Current perspectives on stability of protein drug products during formulation, fill and finish operations. Biotechnol Prob 24:504-514.
8. Bee JS, Randolph TW, Carpenter JF, Bishop S, Dimitrova M. 2011. Effects of surfaces and leachables on the stability of biopharmaceuticals. J Pharm Sci 100:4158-4170.
9. Bee JS, Stevenson JL, Mehta B, Svitel J, Pollastrini J, Platz R, Freund E, Carpenter JF, Randolph TW. 2009. Response of a concentrated monoclonal antibody formulation to high shear. Biotechnol Bioeng 103:936-943.
10. Shire S. 2009. Formulation and manufacturability of biologics. Curr Opin Biotechnol 20:708-714.
11. Eugene J, McNally C. 1999. The importance of a thorough preformulation study. In Protein formulation and delivery; McNally E, Ed. New York: Marcel Dekker, pp 111-138.
12. Strambini GB, Gabellieri E. 1996. Proteins in frozen solutions: Evidence of ice-induced partial unfolding. Biophys J 70:971-976.
13. Bhatnagar BS, Bogner RH, Pikal MJ. 2007. Protein stability during freezing: Separation of stresses and mechanisms of protein stabilization. Pharm Dev Technol 12:505-523.
14. Hawe A, Kasper JC, Friess W, Jiskoot W. 2009. Structural properties of monoclonal antibody aggregates induced by freeze-thawing and thermal stress. Eur J Pharm Sci 38:79-87.
15. Joubert MK, Luo Q, Nashed-Samuel Y, Wypych J, Narhi LO. 2011. Classification and characterization of therapeutic antibody aggregates. J Biolog Chem 286:25118-25133.
16. Fradkin AH, Carpenter JF, Randolph TW. 2009. Immunogenicity of aggregates in recombinant human growth hormone in mouse models. J Pharm Sci 98:3247-3264.
17. Kiese S, Pappenberger A, Friess W, Mahler H-C. 2008. Shaken, not stirred: Mechanical stress testing of an IgG1 antibody. J Pharm Sci 97:4347-4366.
18. Ishikawa T, Kobayashi N, Osawa C, Sawa E, Wakamatsu K. 2010. Prevention of stirring-induced microparticle formation in monoclonal antibody solutions. Biol Pharm Bull 33:1043-1046.
19. Philo JS. 2009. A critical review of methods for size characterization of non-particulate protein aggregates. Curr Pharm Biotechnol 10:359-372.
20. Rosenberg A. 2006. Effects of protein aggregates: An immunologic perspective. AAPS J 8:501-507.
21. Carpenter JF, Randolph TW, Jiskoot W, Crommelin DJA, Middaugh CR, Winter G, Fan Y-X, Kirshner S, Verthelyi D, Kozlowski S, Clouse KA, Swann PG, Rosenberg A, Cherny B. 2009. Overlooking subvisible particles in therapeutic protein products: Gaps that may compromise product quality. J Pharm Sci 98:1201-1205.
22. Fradkin AH, Carpenter JF, Randolph TW. 2011. Glass particles as an adjuvant: A model for adverse immunogenicity of therapeutic proteins. J Pharm Sci 100:4953-4964.
23. Barnard JG, Singh S, Randolph TW, Carpenter JF. 2011. Subvisible particle counting provides a sensitive method of detecting and quantifying aggregation of monoclonal antibody caused by freeze-thawing: Insights into the roles of particles in the protein aggregation pathway. J Pharm Sci 100:492-503.
24. Pace CN. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131:266-280.
25. Myers JK, Pace CN, Scholtz JM. 1995. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding. Protein Sci 4:2138-2148.
26. Faude A, Zacher D, Muller E, Bottinger H. 2007. Fast determination of conditions for maximum dynamic capacity in cation-exchange chromatography of human monoclonal antibodies. J Chromatogr A 1161:29-35.
27. Berg JM, Tymoczko JL, Stryer L. 2002. Protein structure and function. In Biochemistry. New York: W.H. Freeman and Company, pp 41-73.
28. Steadman BL, Thompson KC, Middaugh CR, Matsuno K, Vrona S, Lawson EQ, Lewis RV. 1991. The effects of surface adsorption on the thermal stability of proteins. Biotechnol Bioeng 40:8-15.
29. Katakam M, Bell LN, Banga AK. 1995. Effect of surfactants on the physical stability of recombinant human growth hormone. J Pharm Sci 84:713-716.
30. Bam NB, Cleland JL, Yang J, Manning MC, Carpenter JF, Kelley RF, Randolph TW. 1998. Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions. J Pharm Sci 87:1554-1559.
31. Majumdar S, Ford BM, Mar KD, Sullivan VJ, Ulrich RG, D'Souza AJM. 2011. Evaluations of the effect of syringe surfaces on protein formulations. J Pharm Sci 100:2563-2573.
32. Jaspe J, Hagen SJ. 2006. Do protein molecules unfold in a simple shear flow? Biophys J 91:3415-3424.
33. Thomas CR, Geer D. 2011. Effects of shear on proteins in solution. Biotechnol Lett 33:443-456.
34. Maa Y-F, Hsu CC. 1997. Protein denaturation by combined effect of shear and air-liquid interface. Biotechnol Bioeng 54:503-512.