Aggregation factor analysis for protein formulation by a systematic approach using FTIR, SEC and design of experiments techniques

Journal of Pharmaceutical and Biomedical Analysis

Volumn 57, Issue 1, 2012, Pages 143-152

  Feng, Yan Wen ^a   Ooishi, Ayako ^a   Honda, Shinya ^a  

^a NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

Accelerated testing; Antibody drug; D optimal design; Human immunoglobulin G; Stress testing

Indexed keywords

EXCIPIENT; IMMUNOGLOBULIN G; PHOSPHATE; POLYCLONAL ANTIBODY; POLYSORBATE 80; PROTEIN; SODIUM CHLORIDE; SUCROSE;

ARTICLE; CONCENTRATION RESPONSE; DRUG DESIGN; DRUG FORMULATION; DRUG STORAGE; FACTORIAL ANALYSIS; GEL PERMEATION CHROMATOGRAPHY; INFRARED SPECTROSCOPY; MECHANICAL STRESS; MOLECULAR INTERACTION; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN STABILITY; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

CHROMATOGRAPHY, GEL; FACTOR ANALYSIS, STATISTICAL; HYDROGEN-ION CONCENTRATION; PROTEIN CONFORMATION; PROTEINS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE;

EID: 80054024949     PISSN: 07317085     EISSN: 1873264X     Source Type: Journal    
DOI: 10.1016/j.jpba.2011.08.035     Document Type: Article

References (30)

1. Wang W., Roberts C.J. Aggregation of Therapeutic Proteins 2010, A John Wiley & Sons, Inc., New Jersey.
2. Kendrick B.S., Carpenter J.F., Cleland J.L., Randolph T.W. A transient expansion of the native state precedes aggregation of recombinant human interferon-gamma. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:14142-14146.
3. Mahler H.C., Müller R., Friess W., Delille A., Matheus S. Induction and analysis of aggregates in a liquid IgG1-antibody formulation. Eur. J. Pharm. Biopharm. 2005, 59:407-417.
4. Szenczi Á., Kardos J., Medgyesi G.A., Závodszky P. The effect of solvent environment on the conformation and stability of human polyclonal IgG in solution. Biologicals 2006, 34:5-14.
5. Matheus S., Mahler H.C., Friess W. A critical evaluation of Tm (FTIR) measurements of high-concentration IgG1 antibody formulations as a formulation development tool. Pharm. Res. 2006, 23:1617-1627.
6. Ahrer K., Buchacher A., Iberer G., Jungbauer A. Thermodynamic stability and formation of aggregates of human immunoglobulin G characterized by differential scanning calorimetry and dynamic light scattering. J. Biochem. Biophys. Methods 2006, 66:73-86.
7. Bolli R., Woodtli K., Bärtschi M., Höfferer L., Lerch P. l-Proline reduces IgG dimmer content and enhances the stability of intravenous immunoglobulin (IVIG) solution. Biologicals 2010, 38:150-157.
8. Wang W. Protein aggregation and its inhibition in biopharmaceutics. Int. J. Pharm. 2005, 289:1-30.
9. Capelle M.A.H., Gurny R., Arvinte T. High throughput screening of protein formulation stability: practical considerations. Eur. J. Pharm. Biopharm. 2007, 65:131-148.
10. Wang W., Wang Y.J., Wang D.Q. Dual effects of Tween 80 on protein stability. Int. J. Pharm. 2008, 34:731-738.
11. Philo J.S. Is any measurement method optimal for all aggregate sizes and types?. AAPS J. 2006, 8:564-571.
12. Vonhoff S., Condliffe J., Schiffer H. Implementation of an FTIR calibration curve for fast and objective determination of changes in protein secondary structure during formulation development. J. Pharm. Biomed. Anal. 2010, 50:39-45.
13. Zscherp C., Aygun H., Engels J.W., Mantele W. Effect of proline to alanine mutation on the thermal stability of the all-beta-sheet protein tendamistat. Biochim. Biophys. Acta 2003, 1651:139-145.
14. Fabian H., Schultz C., Backman J., Hahn U., Saenger W., Mantsch H.H., Naumann D. Impact of point mutations on the structure and thermal stability of ribonuclease T1 in aqueous solution probed by Fourier transform infrared spectroscopy. Biochemistry 1994, 33:10725-10730.
15. Jackson M., Mantsch H.H. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 1995, 30:95-120.
16. Ventrella A., Catucci L., Villari V., Scolaro L.M., Agostiano A. Focus on the aggregation processes of photosystem II complexes. Bioelectrochemistry 2007, 70:33-38.
17. Ruddon R.W., Bedows E. Assisted protein folding. J. Biol. Chem. 1997, 272:3125-3128.
18. Gu L.C., Erdos E.A., Chiang H.S., Calderwood T., Tsai K., Visor G.C., Duffy J., Hsu W.C., Foster L.C. Stability of interleukin 1 beta (IL-1 beta) in aqueous solution: analytical methods, kinetics, products, and solution formulation implications. Pharm. Res. 1991, 8:485-490.
19. Vrkljan M., Foster T.M., Powers M.E., Henkin J., Porter W.R., Staack H., Carpenter J.F., Manning M.C. Thermal stability of low molecular weight urokinase during heat treatment. II. Effect of polymeric additives. Pharm. Res. 1994, 11:1004-1008.
20. Won C.W., Molnar T.E., McKean R.E., Spenlehauer G.A. Stabilizers against heat-induced aggregation of RPR 114849, an acidic fibroblast growth factor (aFGF). Int. J. Pharm. 1998, 167:25-36.
21. Pikal M.J., Dellerman K.M., Roy M.L., Riggin R.M. The effects of formulation variables on the stability of freeze-dried human growth hormone. Pharm. Res. 1991, 8:427-436.
22. Arakawa T., Prestrelski S.J., Kenney W.C., Carpenter J.F. Factors affecting short-term and long-term stabilities of proteins. Adv. Drug Deliv. Rev. 1993, 10:1-28.
23. Chen H.K., Yeung A., Gonda K.L. Effects of additives on heat denaturation of rhDNase in solutions. Pharm. Res. 1996, 13:756-761.
24. Treuheit M.J., Kosky A.A., Brems D.N. Inverse relationship of protein concentration and aggregation. Pharm. Res. 2002, 19:511-516.
25. Ishikawa T., Ito T., Endo R., Nakagawa K., Wakamatsu E.S.K. Influence of pH on heat-induced aggregation and degradation of therapeutic monoclonal antibodies. Biol. Pharm. Bull. 2010, 33:1413-1417.
26. Arosio P., Barolo G., Müller-Späth T., Wu H., Morbidelli M. Aggregation stability of a monoclonal antibody during downstream processing. Pharm. Res. 2011, 28:1884-1894.
27. Capelle M.A.H., Gurny R., Arvinte T. A high throughput protein formulation platform: case study of Salmon Calcitonin. Pharm. Res. 2009, 26:118-128.
28. Li Y., Mach H., Blue J.T. High throughput formulation screening for global aggregation behaviors of three monoclonal antibodies. J. Pharm. Sci. 2011, 100:2120-2135.
29. Goldberg D.S., Bishop S.M., Shan A.U., Sathish H.A. Formulation development of therapeutic monoclonal antibodies using high throughput fluorescence and static light scattering techniques: role of conformational and colloidal stability. J. Pharm. Sci. 2011, 100:1306-1315.
30. He F., Woods C., Trilisky E., Bower K.M., Litowski J.R., Kerwin B.A., Becker G.W., Narhi L.O., Razinkov V.I. Screening of monoclonal antibody formulations based on high throughput thermostability and viscosity measurements: design of experiment and statistical analysis. J. Pharm. Sci. 2011, 100:1330-1340.