Analytical approaches to assess the degradation of therapeutic proteins

TrAC - Trends in Analytical Chemistry

Volumn 49, Issue , 2013, Pages 118-125

  Filipe, Vasco ^a   Hawe, Andrea ^b   Carpenter, John F ^c   Jiskoot, Wim ^a  

^a LEIDEN UNIVERSITY   (Netherlands)

^b Coriolis Pharma ^*  (Germany)

^c UNIVERSITY OF COLORADO   (United States)

Author keywords

Analytical technique; Chemical change; Conformational change; Degradation; Drug; Instability; Product development; Protein aggregate; Protein degradation; Therapeutic protein

Indexed keywords

CHEMICAL ANALYSIS; DEGRADATION; PLASMA STABILITY; PRODUCT DEVELOPMENT;

ANALYTICAL TECHNIQUE; CHEMICAL CHANGE; CONFORMATIONAL CHANGE; DRUG; PROTEIN AGGREGATES; PROTEIN DEGRADATION; THERAPEUTIC PROTEIN;

PROTEINS;

AMINO TERMINAL TELOPEPTIDE; ASPARTIC ACID; CYSTEINE; GLUTAMIC ACID; GLYCINE; HISTIDINE; METHIONINE;

ANALYTIC METHOD; ASYMMETRICAL FLOW FIELD FLOW FRACTIONATION; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; DYNAMIC SCANNING FLUOROMETRY; ELECTRICAL ZONE SENSING; ENZYME ACTIVITY; FLUORESCENCE ACTIVATED PARTICLE SORTING; FLUOROMETRY; GEL PERMEATION CHROMATOGRAPHY; INFRARED SPECTROSCOPY; LIGHT SCATTERING; NANOPARTICLE TRACKING ANALYSIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DEGRADATION; RESONANT MASS MEASUREMENT; REVIEW; ULTRACENTRIFUGATION;

EID: 84881252251     PISSN: 01659936     EISSN: 18793142     Source Type: Journal    
DOI: 10.1016/j.trac.2013.05.005     Document Type: Review

References (50)

1. Walsh G. Biopharmaceutical benchmarks. Nat. Biotechnol. 2010, 28(2010):917-924.
2. Schellekens H. The immunogenicity of therapeutic proteins. Discov. Med. 2010, 9:560-564.
3. Chirmule N., Jawa V., Meibohm B. Immunogenicity to therapeutic proteins: impact on PK/PD and efficacy. AAPS J. 2012, 14:296-302.
4. Jiskoot W., Randolph T.W., Volkin D.B., Middaugh C.R., Schöneich C., Winter G., Friess W., Crommelin D.J., Carpenter J.F. Protein instability and immunogenicity: roadblocks to clinical application of injectable protein delivery systems for sustained release. J. Pharm. Sci. 2012, 101:946-954.
5. Cromwell M.E., Hilario E., Jacobson F. Protein aggregation and bioprocessing. AAPS J. 2006, 8:E572-E579.
6. Wang W. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int. J. Pharm. 1999, 185:129-188.
7. Manning M.C., Chou D.K., Murphy B.M., Payne R.W., Katayama D.S. Stability of protein pharmaceuticals: an update. Pharm. Res. 2010, 27:544-575.
8. Rosenberg A.S. Effects of protein aggregates: an immunologic perspective. AAPS J. 2006, 8:E501-E507.
9. Hermeling S., Crommelin D.J., Schellekens H., Jiskoot W. Structure-immunogenicity relationships of therapeutic proteins. Pharm. Res. 2004, 21:897-903.
10. Wang W., Nema S., Teagarden D. Protein aggregation-pathways and influencing factors. Int. J. Pharm. 2010, 390:89-99.
11. Mahler H.C., Friess W., Grauschopf U., Kiese S. Protein aggregation: pathways, induction factors and analysis. J. Pharm. Sci. 2009, 98:2909-2934.
12. Joubert M.K., Luo Q., Nashed-Samuel Y., Wypych J., Narhi L.O. Classification and characterization of therapeutic antibody aggregates. J. Biol. Chem. 2011, 286:25118-25133.
13. den Engelsman J., Garidel P., Smulders R., Koll H., Smith B., Bassarab S., Seidl A., Hainzl O., Jiskoot W. Strategies for the assessment of protein aggregates in pharmaceutical biotech product development. Pharm. Res. 2011, 28:920-933.
14. Zölls S., Tantipolphan R., Wiggenhorn M., Winter G., Jiskoot W., Friess W., Hawe A. Particles in therapeutic protein formulations, part 1: overview of analytical methods. J. Pharm. Sci. 2012, 101:914-935.
15. Philo J.S. A critical review of methods for size characterization of non-particulate protein aggregates. Curr. Pharm. Biotechnol. 2009, 10:359-372.
16. Narhi L.O., Jiang Y., Cao S., Benedek K., Shnek D. A critical review of analytical methods for sub-visible and visible particles. Curr. Pharm. Biotechnol. 2009, 10:373-381.
17. United States Pharmacopeia <788> thirty-sixth ed., United States Pharmacopeial Convention, 2013.
18. European Pharmacopeia, seventh ed., European directorate for the quality of medicine, 2.9.19/20 Particulate contamination: visible/sub-visible particles, 2011.
19. Japanese Pharmacopeia, sixteenth ed., Pharmaceuticals and Medical Devices Agency, 6.06/07 Foreign/particulate insoluble matter, 2011.
20. Sharma D.K., King D., Oma P., Merchant C. Micro-flow imaging: flow microscopy applied to sub-visible particulate analysis in protein formulations. AAPS J. 2010, 12:455-464.
21. Filipe V., Hawe A., Jiskoot W. Critical evaluation of nanoparticle tracking analysis (NTA) by nanosight for the measurement of nanoparticles and protein aggregates. Pharm. Res. 2010, 27:796-810.
22. Rhyner M.N. The Coulter principle for analysis of sub-visible particles in protein formulations. AAPS J. 2011, 13:54-58.
23. Filipe V., Poole R., Oladunjoye O., Braeckmans K., Jiskoot W. Detection and characterization of sub-visible aggregates of monoclonal IgG in serum. Pharm. Res. 2012, 29:2202-2212.
24. Kim Y.S., Randolph T.W., Manning M.C., Stevens F.J., Carpenter J.F. Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation. J. Biol. Chem. 2003, 278:10842-10850.
25. Hawe A., Friess W., Sutter M., Jiskoot W. Online fluorescent dye detection method for the characterization of immunoglobulin G aggregation by size exclusion chromatography and asymmetrical flow field flow fractionation. Anal. Biochem. 2008, 378:115-122.
26. Pekar A., Sukumar M. Quantitation of aggregates in therapeutic proteins using sedimentation velocity analytical ultracentrifugation: practical considerations that affect precision and accuracy. Anal. Biochem. 2007, 367:225-237.
27. Hawe A., Romeijn S., Filipe V., Jiskoot W. Asymmetrical flow field-flow fractionation method for the analysis of submicron protein aggregates. J. Pharm. Sci. 2012, 101:4129-4139.
28. Greenfield N.J. Using circular dichroism spectra to estimate protein secondary structure. Nat. Protoc. 2006, 1:2876-2890.
29. Kong J., Yu S. Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta. Biochim. Biophys. Sin. (Shanghai) 2007, 39:549-559.
30. Lin K., Yang H., Gao Z., Li F., Yu S. Overestimated accuracy of circular dichroism in determining protein secondary structure. Eur. Biophys. J. 2013.
31. Khrapunov S. Circular dichroism spectroscopy has intrinsic limitations for protein secondary structure analysis. Anal. Biochem. 2009, 389:174-176.
32. 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.
33. Li C.H., Nguyen X., Narhi L., Chemmalil L., Towers E., Muzammil S., Gabrielson J., Jiang Y. Applications of circular dichroism (CD) for structural analysis of proteins: qualification of near- and far-UV CD for protein higher order structural analysis. J. Pharm. Sci. 2011, 100:4642-4654.
34. Abbas S.A., Gaspar G., Sharma V.K., Patapoff T.W., Kalonia D.S. Application of second-derivative fluorescence spectroscopy to monitor subtle changes in a monoclonal antibody structure. J. Pharm. Sci. 2013, 102:52-61.
35. Hawe A., Sutter M., Jiskoot W. Extrinsic fluorescent dyes as tools for protein characterization. Pharm. Res. 2008, 25:1487-1499.
36. Johnson C.M. Differential scanning calorimetry as a tool for protein folding and stability. Arch. Biochem. Biophys. 2013, 531:100-109.
37. He F., Woods C.E., 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. 2010.
38. Hawe A., Filipe V., Jiskoot W. Fluorescent molecular rotors as dyes to characterize polysorbate-containing IgG formulations. Pharm. Res. 2010, 27:314-326.
39. Hermeling S., Aranha L., Damen J.M., Slijper M., Schellekens H., Crommelin D.J., Jiskoot W. Structural characterization and immunogenicity in wild-type and immune tolerant mice of degraded recombinant human interferon alpha2b. Pharm. Res. 2005, 22:1997-2006.
40. Filipe V., Jiskoot W., Basmeleh A.H., Halim A., Schellekens H., Brinks V. Immunogenicity of different stressed IgG monoclonal antibody formulations in immune tolerant transgenic mice. MAbs 2012, 4:740-752.
41. Shacter E. Quantification and significance of protein oxidation in biological samples. Drug. Metab. Rev. 2000, 32:307-326.
42. Domon B., Aebersold R. Mass spectrometry and protein analysis. Science 2006, 312:212-217.
43. Zhang Z., Pan H., Chen X. Mass spectrometry for structural characterization of therapeutic antibodies. Mass. Spectrom. Rev. 2009, 28:147-176.
44. Philo J.S. Is any measurement method optimal for all aggregate sizes and types?. AAPS J. 2006, 8:E564-E571.
45. Hawe A., Wiggenhorn M., van de Weert M., Garbe J.H., Mahler H.C., Jiskoot W. Forced degradation of therapeutic proteins. J. Pharm. Sci. 2012, 101:895-913.
46. Fast J.L., Cordes A.A., Carpenter J.F., Randolph T.W. Physical instability of a therapeutic Fc fusion protein: domain contributions to conformational and colloidal stability. Biochemistry 2009, 48:11724-11736.
47. Kim J.H., Iyer V., Joshi S.B., Volkin D.B., Middaugh C.R. Improved data visualization techniques for analyzing macromolecule structural changes. Protein Sci. 2012, 21:1540-1553.
48. Maddux N.R., Joshi S.B., Volkin D.B., Ralston J.P., Middaugh C.R. Multidimensional methods for the formulation of biopharmaceuticals and vaccines. J. Pharm. Sci. 2011.
49. Easter B.R., Sutton D.A., Drewes S.E. Crystalline [A21-desamido]bovine insulin. Hoppe Seylers Z. Physiol. Chem. 1978, 359:1229-1236.
50. Moslemi P., Najafabadi A.R., Tajerzadeh H. A rapid and sensitive method for simultaneous determination of insulin and A21-desamido insulin by high-performance liquid chromatography. J. Pharm. Biomed. Anal. 2003, 33:45-51.