Effect of microencapsulation shear stress on the structural integrity and biological activity of a model monoclonal antibody, trastuzumab

Pharmaceutics

Volumn 3, Issue 3, 2011, Pages 510-524

  Pabari, Ritesh M ^a   Ryan, Benedict ^a   McCarthy, Catherine ^a   Ramtoola, Zebunnissa ^a  

^a ROYAL COLLEGE OF SURGEONS IN IRELAND   (Ireland)

Author keywords

Biological activity; Circular dichroism; Shear stress; Size exclusion chromatography; Stability; Trastuzumab

Indexed keywords

DRUG CARRIER; EPIDERMAL GROWTH FACTOR RECEPTOR 2; MICROPARTICLE; NANOPARTICLE; TRASTUZUMAB; UNCLASSIFIED DRUG;

ANTINEOPLASTIC ACTIVITY; ARTICLE; BIOLOGICAL ACTIVITY; CANCER CELL CULTURE; CANCER INHIBITION; CELL PROLIFERATION; CIRCULAR DICHROISM; CONTROLLED STUDY; DRUG STABILITY; DRUG STRUCTURE; FREEZE DRYING; FREEZE THAWING; GEL ELECTROPHORESIS; GEL PERMEATION CHROMATOGRAPHY; HUMAN; HUMAN CELL; MICROENCAPSULATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN EXPRESSION; SHEAR STRESS; SPRAY DRYING; ULTRASOUND;

EID: 80052973440     PISSN: None     EISSN: 19994923     Source Type: Journal    
DOI: 10.3390/pharmaceutics3030510     Document Type: Article

References (34)

1. Romond, E.H.; Perez, E.A.; Bryant, J.; Suman, V.J.; Geyer, C.E., Jr.; Davidson, N.E.; Tan-Chiu, E.; Martino, S.; Paik, S.; Kaufman, P.A.; Swain, S.M.; Pisansky, T.M.; Fehrenbacher, L.; Kutteh, L.A.; Vogel, V.G.; Visscher, D.W.; Yothers, G.; Jenkins, R.B.; Brown, A.M.; Dakhil, S.R.; Mamounas, E.P.; Lingle, W.L.; Klein, P.M.; Ingle, J.N.; Wolmark, N. Trastuzumab plus adjuvant chemotherapy for operable HER2-positive breast cancer. N. Engl. J. Med. 2005, 353, 1673-1684.
2. Biddlecombe, J.G.; Smith, G.; Uddin, S.; Mulot, S.; Spencer, D.; Gee, C.; Fish, B.C.; Bracewell, D.G. Factors influencing antibody stability at solid-liquid interfaces in a high shear environment. Biotechnol. Prog. 2009, 25, 1499-1507.
3. Kiese, S.; Papppenberger, A.; Friess, W.; Mahler, H.C. Shaken, not stirred: mechanical stress testing of an IgG1 antibody. J. Pharm. Sci. 2008, 97, 4347-4366.
4. Paborji, M.; Pochopin, N.L.; Coppola, W.P.; Bogardus, J.B. Chemical and Physical Stability of Chimeric L6, a Mouse-Human Monoclonal Antibody. Pharm. Res. 1994, 11, 764-771.
5. Vermeer, A.W.P.; Bremer, M.G.E.G.; Norde, W. Structural changes of IgG induced by heat treatment and by adsorption onto a hydrophobic Teflon surface studied by circular dichroism spectroscopy. Biochim. Biophys. Acta 1998, 1425, 1-12.
6. Li, S.Q.; Bomser, J.A.; Zhang, Q.H. Effects of pulsed electric fields and heat treatment on stability and secondary structure of bovine immunoglobulin G. J. Agric. Food Chem. 2005, 53, 663-670.
7. Shire, S.J.; Shahrokh, Z.; Liu, J. Challenges in the development of high protein concentration formulations. J. Pharm. Sci. 2004, 93, 1390-1402.
8. Sluzky, V.; Tamada, J.A.; Klibanov, A.M.; Langer, R. Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces. Proc. Natl. Acad. Sci. USA 1991, 88, 9377-9381.
9. 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 stabilization. Biotechnol. J. 2009, 4, 1305-1319.
10. Lahlou, A.; Blanchet, B.; Carvalho, M.; Paul, M.; Astier, A. Mechanically-induced aggregation of the monoclonal antibody cetuximab. Ann. Pharm. Fr. 2009, 67, 340-352.
11. Stathopulos, P.B.; Scholz, G.A.; Hwang, Y.M.; Rumfeldt, J.A.O.; Lepock, J.R.; Meiering, E.M. Sonication of proteins causes formation of aggregates that resemble amyloid. Protein Sci. 2004, 13, 3017-3027.
12. Chang, B.S.; Kendrick, B.S.; Carpenter, J.F. Surface induced denaturation of proteins during freezing and its inhibition by surfactants. J. Pharm. Sci. 1996, 85, 1325-1330.
13. Ejima, D.; Tsumoto, K.; Fukada, H.; Yumioka, R.; Nagase, K.; Arakawa, T.; Philo, J.S. Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies. Proteins 2007, 66, 954-962.
14. Brange, J.; Havelund, S.; Hougaard, P. Chemical stability of insulin. 2. Formation of higher molecular weight transformation products during storage of pharmaceutical preparations. Pharm. Res. 1992, 9, 727-734.
15. Mahler, H.C.; Friess, W.; Grauschopf, U.; Kiese, S. Protein aggregation: Pathways, induction factors and analysis. J. Pharm. Sci. 2009, 98, 2909-2934.
16. Wang, W.; Singh, S.; Zeng, D.L.; King, K.; Nema, S. Antibody structure, instability, and formulation. J. Pharm. Sci. 2007, 96, 1-26.
17. Cleland, J.L.; Powell, M.F.; Shire, S.J. The development of stable protein formulations: a close look at protein aggregation, deamidation, and oxidation. Crit. Rev. Ther. Drug Carr. S. 1993, 10, 307-377.
18. Ryan, M.E.; Webster, M.L.; Statler, J.D. Adverse effects of intravenous immunoglobulin therapy. Clin. Pediatr. (Phila) 1996, 35, 23-31.
19. Douglas, S.J.; Davis, S.S.; Illum, L. Nanoparticles in drug delivery. Crit. Rev. Ther. Drug Carr. S. 1987, 3, 233-261.
20. Kopecek, J.; Kopeckova, P.; Minko, T.; Lu, Z.R; Peterson, C. Water soluble polymers in tumor targeted delivery. J. Control. Release 2001, 74, 147-158.
21. Peer, D.; Karp, J.M.; Hong, S.; Farokhzad, O.C.; Margalit, R.; Langer, R. Nanocarriers as an emerging platform for cancer therapy. Nat. Nanotechnol. 2007, 2, 751-760.
22. Carter, P.; Presta, L.; Gorman, C.M.; Ridgway, J.; Henner, D; Wong, WL.; Rowland, A.M.; Kotts, C.; Carver, M.E.; Shepard, H.M. Humanization of an anti-p185HER2 antibody for human cancer therapy. Proc. Natl. Acad. Sci. USA 1992, 89, 4285-4289.
23. Hubalek, M.; Brunner, C.; Matthä, K.; Marth, C. Resistance to HER2-targeted therapy: mechanisms of trastuzumab resistance and possible strategies to overcome unresponsiveness to treatment. Wien. Med. Wochenschr. 2010, 160, 506-512.
24. Ramtoola, Z.; Lyons, P.; Keohane, K.; Kerrigan, S.; Kirby, B.; Kelly, J. Investigation of the interaction of biodegradable micro-and nanoparticulate drug delivery systems with platelets. J. Pharm. Pharmacol. 2011, 63, 26-32.
25. Invitrogen. Available online: http://tools.invitrogen.com/content/sfs/manuals/nupage_minigel_qrc.pdf. (accessed on 20 March 2010).
26. Tang, Y.; Wang, J.; Scollard, D.A.; Mondal, H.; Holloway, C.; Kahn, H.J.; Reilly, R.M. Imaging of HER2/neu-positive BT-474 human breast cancer xenografts in athymic mice using 111In-trastuzumab (Herceptin) Fab fragments. Nucl. Med. Biol. 2005, 32, 51-58.
27. Ozbay, T.; Durden, D.L.; Liu, T.; O'Regan, R.M.; Nahta, R. In vitro evaluation of pan-PI3-kinase inhibitor SF1126 in trastuzumab-sensitive and trastuzumab-resistant HER2-over-expressing breast cancer cells. Cancer Chemother. Pharmacol. 2010, 65, 697-706.
28. Krishnamurthy, R.; Lumpkin, J.A.; Sridhar, R. Inactivation of lysozyme by sonication under conditions relevant to microencapsulation. Int. J. Pharm. 2000, 205, 23-34.
29. Pikal-Cleland, K.A.; Rodriguez-Hornedo, N.; Amidon, G.L.; Carpenter, J.F. Protein denaturation during freezing and thawing in phosphate buffer systems: monomeric and tetrameric [beta]-galactosidase. Arch. Biochem. Biophys. 2000, 384, 398-406.
30. Barnard, J.G.; Singh, S.; Randolph, T.W.; Carpenter, J.F. 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. 2010, 100, 492-503.
31. 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, 1952-1960.
32. Adler, M.; Lee, G. Stability and surface activity of lactate dehydrogenase in spray dried trehalose. J. Pharm. Sci. 1999, 88, 199-208.
33. Ye, H. Simultaneous determination of protein aggregation, degradation, and absolute molecular weight by size exclusion chromatography-multiangle laser light scattering. Anal. Biochem. 2006, 356, 76-85.
34. van de Weert, M.; Hennink, W.E.; Jiskoot, W. Protein instability in poly (lactic-co-glycolic acid) microparticles. Pharm. Res. 2000, 17, 1159-1167.