메뉴 건너뛰기




Volumn 100, Issue 12, 2011, Pages 5126-5141

High-throughput assessment of thermal and colloidal stability parameters for monoclonal antibody formulations

Author keywords

Design of experiment; High concentration; High throughput technologies; Monoclonal antibody; Protein aggregation; Protein formulation; Stability; Thermal analysis

Indexed keywords

MONOCLONAL ANTIBODY; OLIGOMER;

EID: 80054935483     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.22712     Document Type: Article
Times cited : (92)

References (37)
  • 1
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An immunologic perspective
    • Rosenberg AS. 2006. Effects of protein aggregates: An immunologic perspective. AAPS J 8(3):E501-E507.
    • (2006) AAPS J , vol.8 , Issue.3
    • Rosenberg, A.S.1
  • 2
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization, and formulation of liquid protein pharmaceuticals
    • Wang W. 1999. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int J Pharm 185(2):129-188.
    • (1999) Int J Pharm , vol.185 , Issue.2 , pp. 129-188
    • Wang, W.1
  • 4
    • 14844334231 scopus 로고    scopus 로고
    • Induction and analysis of aggregates in a liquid IgG1-antibody formulation
    • Mahler HC, Muller R, Friess W, Delille A, Matheus S. 2005. Induction and analysis of aggregates in a liquid IgG1-antibody formulation. Eur J Pharm Biopharm 59(3):407-417.
    • (2005) Eur J Pharm Biopharm , vol.59 , Issue.3 , pp. 407-417
    • Mahler, H.C.1    Muller, R.2    Friess, W.3    Delille, A.4    Matheus, S.5
  • 6
    • 23444451056 scopus 로고    scopus 로고
    • A GLYmmer of insight into fibril formation
    • Uversky VN. 2005. A GLYmmer of insight into fibril formation. Structure 13(8):1090-1092.
    • (2005) Structure , vol.13 , Issue.8 , pp. 1090-1092
    • Uversky, V.N.1
  • 7
    • 70350068542 scopus 로고    scopus 로고
    • Biophysical and stabilization studies of the Chlamydia trachomatis mouse pneumonitis major outer membrane protein
    • Cai S, He F, Samra HS, de la Maza LM, Bottazzi ME, Joshi SB, Middaugh CR. 2009. Biophysical and stabilization studies of the Chlamydia trachomatis mouse pneumonitis major outer membrane protein. Mol Pharm 6(5):1553-1561.
    • (2009) Mol Pharm , vol.6 , Issue.5 , pp. 1553-1561
    • Cai, S.1    He, F.2    Samra, H.S.3    de la Maza, L.M.4    Bottazzi, M.E.5    Joshi, S.B.6    Middaugh, C.R.7
  • 8
    • 33947544337 scopus 로고    scopus 로고
    • Highly concentrated monoclonal antibody solutions: Direct analysis of physical structure and thermal stability
    • Harn N, Allan C, Oliver C, Middaugh CR. 2007. Highly concentrated monoclonal antibody solutions: Direct analysis of physical structure and thermal stability. J Pharm Sci 96(3):532-546.
    • (2007) J Pharm Sci , vol.96 , Issue.3 , pp. 532-546
    • Harn, N.1    Allan, C.2    Oliver, C.3    Middaugh, C.R.4
  • 9
    • 42449118010 scopus 로고    scopus 로고
    • Immunoglobulin dynamics, conformational fluctuations, and nonlinear elasticity and their effects on stability
    • Kamerzell TJ, Ramsey JD, Middaugh CR. 2008. Immunoglobulin dynamics, conformational fluctuations, and nonlinear elasticity and their effects on stability. J Phys Chem B 112(10):3240-3250.
    • (2008) J Phys Chem B , vol.112 , Issue.10 , pp. 3240-3250
    • Kamerzell, T.J.1    Ramsey, J.D.2    Middaugh, C.R.3
  • 10
    • 0034076282 scopus 로고    scopus 로고
    • The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein
    • Vermeer AW, Norde W. 2000. The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein. Biophys J 78(1):394-404.
    • (2000) Biophys J , vol.78 , Issue.1 , pp. 394-404
    • Vermeer, A.W.1    Norde, W.2
  • 11
    • 0033808323 scopus 로고    scopus 로고
    • The unfolding/denaturation of immunogammaglobulin of isotype 2b and its F(ab) and F(c) fragments
    • Vermeer AW, Norde W, van Amerongen A. 2000. The unfolding/denaturation of immunogammaglobulin of isotype 2b and its F(ab) and F(c) fragments. Biophys J 79(4):2150-2154.
    • (2000) Biophys J , vol.79 , Issue.4 , pp. 2150-2154
    • Vermeer, A.W.1    Norde, W.2    van Amerongen, A.3
  • 12
    • 43249105327 scopus 로고    scopus 로고
    • Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies
    • Ionescu RM, Vlasak J, Price C, Kirchmeier M. 2008. Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies. J Pharm Sci 97(4):1414-1426.
    • (2008) J Pharm Sci , vol.97 , Issue.4 , pp. 1414-1426
    • Ionescu, R.M.1    Vlasak, J.2    Price, C.3    Kirchmeier, M.4
  • 14
    • 67849129183 scopus 로고    scopus 로고
    • High-throughput thermal scanning: A general, rapid dye-binding thermal shift screen for protein engineering
    • Lavinder JJ, Hari SB, Sullivan BJ, Magliery TJ. 2009. High-throughput thermal scanning: A general, rapid dye-binding thermal shift screen for protein engineering. J Am Chem Soc 131(11):3794-3795.
    • (2009) J Am Chem Soc , vol.131 , Issue.11 , pp. 3794-3795
    • Lavinder, J.J.1    Hari, S.B.2    Sullivan, B.J.3    Magliery, T.J.4
  • 15
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • Ericsson UB, Hallberg BM, Detitta GT, Dekker N, Nordlund P. 2006. Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal Biochem 357(2):289-298.
    • (2006) Anal Biochem , vol.357 , Issue.2 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    Detitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 17
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen FH, Berglund H, Vedadi M. 2007. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat Protoc 2(9):2212-2221.
    • (2007) Nat Protoc , vol.2 , Issue.9 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 19
    • 77949789023 scopus 로고    scopus 로고
    • High-throughput thermostability screening of monoclonal antibody formulations
    • He F, Hogan S, Latypov RF, Narhi LO, Razinkov VI. 2010. High-throughput thermostability screening of monoclonal antibody formulations. J Pharm Sci 99(4):1707-1720.
    • (2010) J Pharm Sci , vol.99 , Issue.4 , pp. 1707-1720
    • He, F.1    Hogan, S.2    Latypov, R.F.3    Narhi, L.O.4    Razinkov, V.I.5
  • 20
    • 0027729733 scopus 로고
    • The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation
    • Cleland JL, Powell MF, Shire SJ. 1993. The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation. Crit Rev Ther Drug Carrier Syst 10(4):307-377.
    • (1993) Crit Rev Ther Drug Carrier Syst , vol.10 , Issue.4 , pp. 307-377
    • Cleland, J.L.1    Powell, M.F.2    Shire, S.J.3
  • 23
    • 55749109195 scopus 로고    scopus 로고
    • Shaken, not stirred: Mechanical stress testing of an IgG1 antibody
    • Kiese S, Papppenberger A, Friess W, Mahler HC. 2008. Shaken, not stirred: Mechanical stress testing of an IgG1 antibody. J Pharm Sci 97(10):4347-4366.
    • (2008) J Pharm Sci , vol.97 , Issue.10 , pp. 4347-4366
    • Kiese, S.1    Papppenberger, A.2    Friess, W.3    Mahler, H.C.4
  • 24
    • 31344474356 scopus 로고    scopus 로고
    • Colloidal behavior of proteins: effects of the second virial coefficient on solubility, crystallization and aggregation of proteins in aqueous solution
    • Valente JJ, Payne RW, Manning MC, Wilson WW, Henry CS. 2005. Colloidal behavior of proteins: effects of the second virial coefficient on solubility, crystallization and aggregation of proteins in aqueous solution. Curr Pharm Biotechnol 6(6):427-436.
    • (2005) Curr Pharm Biotechnol , vol.6 , Issue.6 , pp. 427-436
    • Valente, J.J.1    Payne, R.W.2    Manning, M.C.3    Wilson, W.W.4    Henry, C.S.5
  • 25
    • 10044279535 scopus 로고    scopus 로고
    • Determination of second virial coefficient of proteins using a dual-detector cell for simultaneous measurement of scattered light intensity and concentration in SEC-HPLC
    • Bajaj H, Sharma VK, Kalonia DS. 2004. Determination of second virial coefficient of proteins using a dual-detector cell for simultaneous measurement of scattered light intensity and concentration in SEC-HPLC. Biophys J 87(6):4048-4055.
    • (2004) Biophys J , vol.87 , Issue.6 , pp. 4048-4055
    • Bajaj, H.1    Sharma, V.K.2    Kalonia, D.S.3
  • 26
    • 0022351381 scopus 로고
    • The concentration-dependence of macromolecular parameters
    • Harding SE, Johnson P. 1985. The concentration-dependence of macromolecular parameters. Biochem J 231(3):543-547.
    • (1985) Biochem J , vol.231 , Issue.3 , pp. 543-547
    • Harding, S.E.1    Johnson, P.2
  • 27
    • 0013441664 scopus 로고    scopus 로고
    • 1st ed. John Wiley & Sons, Inc., New Jersey.
    • Teraoka I. 2002. Polymer solutions. 1st ed. John Wiley & Sons, Inc., New Jersey.
    • (2002) Polymer solutions.
    • Teraoka, I.1
  • 28
    • 33845965334 scopus 로고    scopus 로고
    • Ultrasonic storage modulus as a novel parameter for analyzing protein-protein interactions in high protein concentration solutions: Correlation with static and dynamic light scattering measurements
    • Saluja A, Badkar AV, Zeng DL, Nema S, Kalonia DS. 2007. Ultrasonic storage modulus as a novel parameter for analyzing protein-protein interactions in high protein concentration solutions: Correlation with static and dynamic light scattering measurements. Biophys J 92(1):234-244.
    • (2007) Biophys J , vol.92 , Issue.1 , pp. 234-244
    • Saluja, A.1    Badkar, A.V.2    Zeng, D.L.3    Nema, S.4    Kalonia, D.S.5
  • 29
    • 76649099495 scopus 로고    scopus 로고
    • Specific interactions in high concentration antibody solutions resulting in high viscosity
    • Yadav S, Liu J, Shire SJ, Kalonia DS. 2010. Specific interactions in high concentration antibody solutions resulting in high viscosity. J Pharm Sci 99(3):1152-1168.
    • (2010) J Pharm Sci , vol.99 , Issue.3 , pp. 1152-1168
    • Yadav, S.1    Liu, J.2    Shire, S.J.3    Kalonia, D.S.4
  • 30
    • 78049344329 scopus 로고    scopus 로고
    • Diffusion and sedimentation interaction parameters for measuring the second virial coefficient and their utility as predictors of protein aggregation
    • Saluja A, Fesinmeyer RM, Hogan S, Brems DN, Gokarn YR. 2010. Diffusion and sedimentation interaction parameters for measuring the second virial coefficient and their utility as predictors of protein aggregation. Biophys J 99(8):2657-2665.
    • (2010) Biophys J , vol.99 , Issue.8 , pp. 2657-2665
    • Saluja, A.1    Fesinmeyer, R.M.2    Hogan, S.3    Brems, D.N.4    Gokarn, Y.R.5
  • 32
    • 79951892441 scopus 로고    scopus 로고
    • Screening of monoclonal antibody formulations based on high-throughput thermostability and viscosity measurements: Design of experiment and statistical analysis
    • He F, Woods CE, Trilisky E, Bower KM, Litowski JR, Kerwin BA, Becker GW, Narhi LO, Razinkov VI. 2010. Screening of monoclonal antibody formulations based on high-throughput thermostability and viscosity measurements: Design of experiment and statistical analysis. J Pharm Sci 100:1330-1340.
    • (2010) J Pharm Sci , vol.100 , pp. 1330-1340
    • He, F.1    Woods, C.E.2    Trilisky, E.3    Bower, K.M.4    Litowski, J.R.5    Kerwin, B.A.6    Becker, G.W.7    Narhi, L.O.8    Razinkov, V.I.9
  • 36
    • 33644499478 scopus 로고    scopus 로고
    • Monitoring protein aggregation during thermal unfolding in circular dichroism experiments
    • Benjwal S, Verma S, Rohm KH, Gursky O. 2006. Monitoring protein aggregation during thermal unfolding in circular dichroism experiments. Protein Sci 15(3):635-639.
    • (2006) Protein Sci , vol.15 , Issue.3 , pp. 635-639
    • Benjwal, S.1    Verma, S.2    Rohm, K.H.3    Gursky, O.4
  • 37
    • 48549086114 scopus 로고    scopus 로고
    • Effects of solution conditions, processing parameters, and container materials on aggregation of a monoclonal antibody during freeze-thawing
    • Kueltzo LA, Wang W, Randolph TW, Carpenter JF. 2008. Effects of solution conditions, processing parameters, and container materials on aggregation of a monoclonal antibody during freeze-thawing. J Pharm Sci 97(5):1801-1812.
    • (2008) J Pharm Sci , vol.97 , Issue.5 , pp. 1801-1812
    • Kueltzo, L.A.1    Wang, W.2    Randolph, T.W.3    Carpenter, J.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.