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Volumn 103, Issue 2, 2014, Pages 437-444

Understanding the relationship between biotherapeutic protein stability and solid-liquid interfacial shear in constant region mutants of IgG1 and IgG4

Author keywords

Biopharmaceuticals characterization; Calorimetry (DSC); IgG antibody; In silico modeling; Molecular modeling; Protein aggregation; Protein structure; Thermal analysis

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G ANTIBODY; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G1 ANTIBODY; IMMUNOGLOBULIN G4; IMMUNOGLOBULIN G4 ANTIBODY; UNCLASSIFIED DRUG;

EID: 84895924014     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23822     Document Type: Article
Times cited : (18)

References (54)
  • 1
    • 34447566117 scopus 로고    scopus 로고
    • Quantitative characterization of weak self-association in concentrated solutions of immunoglobulin G via the measurement of sedimentation equilibrium and osmotic pressure
    • Jimenez M, Rivas Gn, Minton AP. 2007. Quantitative characterization of weak self-association in concentrated solutions of immunoglobulin G via the measurement of sedimentation equilibrium and osmotic pressure. Biochemistry 46(28):8373-8378.
    • (2007) Biochemistry , vol.46 , Issue.28 , pp. 8373-8378
    • Jimenez, M.1    Rivas, G.2    Minton, A.P.3
  • 2
    • 84865353525 scopus 로고    scopus 로고
    • The future of protein particle characterization and understanding its potential to diminish the immunogenicity of biopharmaceuticals: A shared perspective
    • Bee JS, Goletz TJ, Ragheb JA. 2012. The future of protein particle characterization and understanding its potential to diminish the immunogenicity of biopharmaceuticals: A shared perspective. J Pharm Sci 101(10):3580-3585.
    • (2012) J Pharm Sci , vol.101 , Issue.10 , pp. 3580-3585
    • Bee, J.S.1    Goletz, T.J.2    Ragheb, J.A.3
  • 4
    • 0037083944 scopus 로고    scopus 로고
    • Particulatematter contamination of intravenous antibiotics aggravates loss of functional capillary density in postischemic striated muscle
    • Lehr H-A, Brunner J, Rangoonwala R, James Kirkpatrick C. 2002. Particulatematter contamination of intravenous antibiotics aggravates loss of functional capillary density in postischemic striated muscle. Am J Respir Crit Care Med 165(4):514-520.
    • (2002) Am J Respir Crit Care Med , vol.165 , Issue.4 , pp. 514-520
    • Lehr, H.-A.1    Brunner, J.2    Rangoonwala, R.3    James Kirkpatrick, C.4
  • 5
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An immunologic perspective
    • Rosenberg A. 2006. Effects of protein aggregates: An immunologic perspective. AAPS J 8(3):E501-E507.
    • (2006) AAPS J , vol.8 , Issue.3
    • Rosenberg, A.1
  • 9
    • 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
  • 11
    • 69249175069 scopus 로고    scopus 로고
    • Ultraviolet Raman spectroscopy is uniquely suitable for studying amyloid diseases
    • Lednev IK, Shashilov V, Xu M. 2009. Ultraviolet Raman spectroscopy is uniquely suitable for studying amyloid diseases. Curr Sci 97(2):180.
    • (2009) Curr Sci , vol.97 , Issue.2 , pp. 180
    • Lednev, I.K.1    Shashilov, V.2    Xu, M.3
  • 12
    • 84895926816 scopus 로고    scopus 로고
    • Mass spectrometry
    • New Jersey: John Wiley & Sons, Inc.
    • Hammes GG. 2005. Mass spectrometry. Spectroscopy for the biological sciences. New Jersey: John Wiley & Sons, Inc., pp 145-162.
    • (2005) Spectroscopy for the Biological Sciences , pp. 145-162
    • Hammes, G.G.1
  • 13
    • 35348827271 scopus 로고    scopus 로고
    • Determining antibody stability: Creation of solid- liquid interfacial effects within a high shear environment
    • Biddlecombe JG, Craig AV, Zhang H, Uddin S, Mulot S, Fish BC, Bracewell DG. 2007. Determining antibody stability: Creation of solid- liquid interfacial effects within a high shear environment. Biotechnol Progr 23(5):1218-1222.
    • (2007) Biotechnol Progr , vol.23 , Issue.5 , pp. 1218-1222
    • Biddlecombe, J.G.1    Craig, A.V.2    Zhang, H.3    Uddin, S.4    Mulot, S.5    Fish, B.C.6    Bracewell, D.G.7
  • 14
    • 79959868514 scopus 로고    scopus 로고
    • Highthroughput screening of excipients intended to prevent antigen aggregation at air-liquid interface
    • Dasnoy S, Dezutter N, Lemoine D, Le Bras V, Praat V. Highthroughput screening of excipients intended to prevent antigen aggregation at air-liquid interface. Pharm Res 28(7):1591-1605.
    • Pharm Res , vol.28 , Issue.7 , pp. 1591-1605
    • Dasnoy, S.1    Dezutter, N.2    Lemoine, D.3    Le Bras, V.4    Praat, V.5
  • 15
    • 79960128166 scopus 로고    scopus 로고
    • Classification and characterization of therapeutic antibody aggregates
    • Joubert MK, Luo Q, Nashed-Samuel Y, Wypych J, Narhi LO. 2011. Classification and characterization of therapeutic antibody aggregates. J Biol Chem 286(28):25118-25133.
    • (2011) J Biol Chem , vol.286 , Issue.28 , pp. 25118-25133
    • Joubert, M.K.1    Luo, Q.2    Nashed-Samuel, Y.3    Wypych, J.4    Narhi, L.O.5
  • 16
    • 68949119488 scopus 로고    scopus 로고
    • Monoclonal antibody interactions with micro- and nanoparticles: Adsorption, aggregation, and accelerated stress studies
    • Bee JS, Chiu D, Sawicki S, Stevenson JL, Chatterjee K, Freund E, Carpenter JF, Randolph TW. 2009. Monoclonal antibody interactions with micro- and nanoparticles: Adsorption, aggregation, and accelerated stress studies. J Pharm Sci 98(9):3218-3238.
    • (2009) J Pharm Sci , vol.98 , Issue.9 , pp. 3218-3238
    • Bee, J.S.1    Chiu, D.2    Sawicki, S.3    Stevenson, J.L.4    Chatterjee, K.5    Freund, E.6    Carpenter, J.F.7    Randolph, T.W.8
  • 17
    • 79951768234 scopus 로고    scopus 로고
    • Effects of shear on proteins in solution
    • Thomas C, Geer D Effects of shear on proteins in solution. Biotechnol Lett 33(3):443-456.
    • Biotechnol Lett , vol.33 , Issue.3 , pp. 443-456
    • Thomas, C.1    Geer, D.2
  • 18
    • 68749118103 scopus 로고    scopus 로고
    • Structural properties of monoclonal antibody aggregates induced by freeze-thawing and thermal stress
    • 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(2):79-87.
    • (2009) Eur J Pharm Sci , vol.38 , Issue.2 , pp. 79-87
    • Hawe, A.1    Kasper, J.C.2    Friess, W.3    Jiskoot, W.4
  • 19
    • 55749109195 scopus 로고    scopus 로고
    • Shaken, not stirred: Mechanical stress testing of an IgG1 antibody
    • Kiese S, Papppenberger A, Friess W, Mahler H-C. 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
  • 20
    • 67649171018 scopus 로고    scopus 로고
    • Shear-induced deformation of bovine insulin in Couette flow
    • Bekard IB, Dunstan DE. 2009. Shear-induced deformation of bovine insulin in Couette flow. J Phys Chem B 113(25):8453-8457.
    • (2009) J Phys Chem B , vol.113 , Issue.25 , pp. 8453-8457
    • Bekard, I.B.1    Dunstan, D.E.2
  • 21
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi EY, Krishnan S, Randolph TW, Carpenter JF. 2003. Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation. Pharm Res 20(9):1325-1336.
    • (2003) Pharm Res , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 23
    • 14844334231 scopus 로고    scopus 로고
    • Induction and analysis of aggregates in a liquid IgG1-antibody formulation
    • Mahler H-C, Maller R, Friei 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    Maller, R.2    Friei, W.3    Delille, A.4    Matheus, S.5
  • 24
  • 25
    • 33749057744 scopus 로고    scopus 로고
    • Protein aggregation and bioprocessing
    • Cromwell ME, Hilario E, Jacobson F. 2006. Protein aggregation and bioprocessing. AAPS J 8(3):E572-E579.
    • (2006) AAPS J , vol.8 , Issue.3
    • Cromwell, M.E.1    Hilario, E.2    Jacobson, F.3
  • 26
    • 9544258376 scopus 로고    scopus 로고
    • Effect of high shear on proteins
    • Maa Y-F, Hsu CC. 1996. Effect of high shear on proteins. Biotechnol Bioeng 51(4):458-465.
    • (1996) Biotechnol Bioeng , vol.51 , Issue.4 , pp. 458-465
    • Maa, Y.-F.1    Hsu, C.C.2
  • 27
    • 73949093277 scopus 로고    scopus 로고
    • Aggregation of a monoclonal antibody induced by adsorption to stainless steel
    • Bee JS, Davis M, Freund E, Carpenter JF, Randolph TW. 2010. Aggregation of a monoclonal antibody induced by adsorption to stainless steel. Biotechnol Bioeng 105(1):121-129.
    • (2010) Biotechnol Bioeng , vol.105 , Issue.1 , pp. 121-129
    • Bee, J.S.1    Davis, M.2    Freund, E.3    Carpenter, J.F.4    Randolph, T.W.5
  • 29
    • 75749136959 scopus 로고    scopus 로고
    • Feasibility study for the fractionation of the major human immunoglobulin G subclasses using hydrophobic interaction membrane chromatography
    • Wang L, Ghosh R. 2009. Feasibility study for the fractionation of the major human immunoglobulin G subclasses using hydrophobic interaction membrane chromatography. Anal Chem 82(1):452-455.
    • (2009) Anal Chem , vol.82 , Issue.1 , pp. 452-455
    • Wang, L.1    Ghosh, R.2
  • 30
  • 31
    • 0020700160 scopus 로고
    • Serologic aspects of IgG4 antibodies. I. Prolonged immunization results in an IgG4- restricted response
    • Aalberse RC, van der Gaag R, van Leeuwen J. 1983. Serologic aspects of IgG4 antibodies. I. Prolonged immunization results in an IgG4- restricted response. J Immunol 130(2):722-726.
    • (1983) J Immunol , vol.130 , Issue.2 , pp. 722-726
    • Aalberse, R.C.1    Van Der Gaag, R.2    Van Leeuwen, J.3
  • 32
    • 0036161996 scopus 로고    scopus 로고
    • IgG4 breaking the rules
    • Aalberse RC, Schuurman J. 2002. IgG4 breaking the rules. Immunology 105(1):9-19.
    • (2002) Immunology , vol.105 , Issue.1 , pp. 9-19
    • Aalberse, R.C.1    Schuurman, J.2
  • 33
    • 0022995766 scopus 로고
    • Serologic aspects of IgG4 antibodies. II. IgG4 antibodies form small, nonprecipitating immune complexes due to functional monovalency
    • van der Zee JS, van Swieten P, Aalberse RC. 1986. Serologic aspects of IgG4 antibodies. II. IgG4 antibodies form small, nonprecipitating immune complexes due to functional monovalency. J Immunol 137(11):3566-3571.
    • (1986) J Immunol , vol.137 , Issue.11 , pp. 3566-3571
    • Van Der Zee, J.S.1    Van Swieten, P.2    Aalberse, R.C.3
  • 34
    • 36849050718 scopus 로고    scopus 로고
    • Solution conformation of wild-type and mutant IgG3 and IgG4 immunoglobulins using crystallohydrodynamics: Possible implications for complement activation
    • Lu Y, Harding SE, Michaelsen TE, Longman E, Davis KG, Ortega Á, Grossmann JG, Sandlie I, Garća de la Torre J. 2007. Solution conformation of wild-type and mutant IgG3 and IgG4 immunoglobulins using crystallohydrodynamics: Possible implications for complement activation. Biophys J 93(11):3733-3744.
    • (2007) Biophys J , vol.93 , Issue.11 , pp. 3733-3744
    • Lu, Y.1    Harding, S.E.2    Michaelsen, T.E.3    Longman, E.4    Davis, K.G.5    Ortega, Á.6    Grossmann, J.G.7    Sandlie, I.8    De La Torre, G.J.9
  • 35
    • 3543069883 scopus 로고
    • Segmental flexibility and complement fixation of genetically engineered chimeric human, rabbit and mouse antibodies
    • Dangl JL, Wensel TG, Morrison SL, Stryer L, Herzenberg LA, Oi VT. 1988. Segmental flexibility and complement fixation of genetically engineered chimeric human, rabbit and mouse antibodies. EMBO J 7(7):1989-1994.
    • (1988) EMBO J , vol.7 , Issue.7 , pp. 1989-1994
    • Dangl, J.L.1    Wensel, T.G.2    Morrison, S.L.3    Stryer, L.4    Herzenberg, L.A.5    Oi, V.T.6
  • 36
    • 33745823893 scopus 로고    scopus 로고
    • Modulation of the effector functions of a human IgG1 through engineering of its hinge region
    • Dall'Acqua WF, Cook KE, Damschroder MM, Woods RM, Wu H. 2006. Modulation of the effector functions of a human IgG1 through engineering of its hinge region. J Immunol 177(2):1129-1138.
    • (2006) J Immunol , vol.177 , Issue.2 , pp. 1129-1138
    • Dall'Acqua, W.F.1    Cook, K.E.2    Damschroder, M.M.3    Woods, R.M.4    Wu, H.5
  • 37
    • 0021939799 scopus 로고
    • Conformation of human IgG subclasses in solution. Smallangle X-ray scattering and hydrodynamic studies
    • Kilar F, Simon I, Lakatos S, Vonderviszt F, Medgyesi GA, Zavodszky P. 1985. Conformation of human IgG subclasses in solution. Smallangle X-ray scattering and hydrodynamic studies. Eur J Biochem 147(1):17-25.
    • (1985) Eur J Biochem , vol.147 , Issue.1 , pp. 17-25
    • Kilar, F.1    Simon, I.2    Lakatos, S.3    Vonderviszt, F.4    Medgyesi, G.A.5    Zavodszky, P.6
  • 39
    • 64149121224 scopus 로고    scopus 로고
    • Structural characterization of a human Fc fragment engineered for extended serum half-life
    • Oganesyan V, Damschroder MM, Woods RM, Cook KE, Wu H, Dall'Acqua WF. 2009. Structural characterization of a human Fc fragment engineered for extended serum half-life. Mol Immunol 46(8-9):1750-1755.
    • (2009) Mol Immunol , vol.46 , Issue.8-9 , pp. 1750-1755
    • Oganesyan, V.1    Damschroder, M.M.2    Woods, R.M.3    Cook, K.E.4    Wu, H.5    Dall'Acqua, W.F.6
  • 40
    • 33747631571 scopus 로고    scopus 로고
    • Properties of Hhuman IgG1s Eengineered for Eenhanced Bbinding to the Nneonatal Fc Rreceptor (FcRn)
    • Dall'Acqua WF, Kiener PA, Wu H. 2006. Properties of Hhuman IgG1s Eengineered for Eenhanced Bbinding to the Nneonatal Fc Rreceptor (FcRn). J Biol Chem 281(33):23514-23524.
    • (2006) J Biol Chem , vol.281 , Issue.33 , pp. 23514-23524
    • Dall'Acqua, W.F.1    Kiener, P.A.2    Wu, H.3
  • 41
    • 79954531753 scopus 로고    scopus 로고
    • Nonnative aggregation of an IgG1 antibody in acidic conditions: Part 1. Unfolding, colloidal interactions, and formation of highmolecular- weight aggregates
    • Brummitt RK, Nesta DP, Chang L, Chase SF, Laue TM, Roberts CJ. 2011. Nonnative aggregation of an IgG1 antibody in acidic conditions: Part 1. Unfolding, colloidal interactions, and formation of highmolecular- weight aggregates. J Pharm Sci 100(6):2087-2103.
    • (2011) J Pharm Sci , vol.100 , Issue.6 , pp. 2087-2103
    • Brummitt, R.K.1    Nesta, D.P.2    Chang, L.3    Chase, S.F.4    Laue, T.M.5    Roberts, C.J.6
  • 42
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • Roberts CJ. 2007. Non-native protein aggregation kinetics. Biotechnol Bioeng 98(5):927-938.
    • (2007) Biotechnol Bioeng , vol.98 , Issue.5 , pp. 927-938
    • Roberts, C.J.1
  • 44
    • 39749120834 scopus 로고    scopus 로고
    • Amyloid nucleation triggered by agitation of 122-microglobulin under acidic and neutral pH conditions
    • Sasahara K, Yagi H, Sakai M, Naiki H, Goto Y. 2008. Amyloid nucleation triggered by agitation of 122-microglobulin under acidic and neutral pH conditions. Biochemistry 47(8):2650-2660.
    • (2008) Biochemistry , vol.47 , Issue.8 , pp. 2650-2660
    • Sasahara, K.1    Yagi, H.2    Sakai, M.3    Naiki, H.4    Goto, Y.5
  • 45
    • 0037178811 scopus 로고    scopus 로고
    • Kinetics and energetics of assembly, nucleation, and growth of aggregates and fibrils for an amyloidogenic protein
    • Kim Y-S, Randolph TW, Stevens FJ, Carpenter JF. 2002. Kinetics and energetics of assembly, nucleation, and growth of aggregates and fibrils for an amyloidogenic protein. J Biol Chem 277(30) 27240-27246.
    • (2002) J Biol Chem , vol.277 , Issue.30 , pp. 27240-27246
    • Kim, Y.-S.1    Randolph, T.W.2    Stevens, F.J.3    Carpenter, J.F.4
  • 47
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov PL, Potekhin SA. 1986. Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods Enzymol 131:4-51.
    • (1986) Methods Enzymol , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 48
    • 78650099292 scopus 로고    scopus 로고
    • Differential scanning calorimetry techniques: Applications in biology and nanoscience
    • Gill P, Moghadam TT, Ranjbar B. 2010. Differential scanning calorimetry techniques: Applications in biology and nanoscience. J Biomol Tech 21(4):167-193.
    • (2010) J Biomol Tech , vol.21 , Issue.4 , pp. 167-193
    • Gill, P.1    Moghadam, T.T.2    Ranjbar, B.3
  • 49
    • 0034076282 scopus 로고    scopus 로고
    • The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein
    • Vermeer AWP, 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.P.1    Norde, W.2
  • 50
    • 61449121954 scopus 로고    scopus 로고
    • Effect of ions on agitation- and temperature-induced aggregation reactions of antibodies
    • Fesinmeyer R, Hogan S, Saluja A, Brych S, Kras E, Narhi L, Brems D, Gokarn Y. 2009. Effect of ions on agitation- and temperature-induced aggregation reactions of antibodies. Pharm Res 26(4):903-913.
    • (2009) Pharm Res , vol.26 , Issue.4 , pp. 903-913
    • Fesinmeyer, R.1    Hogan, S.2    Saluja, A.3    Brych, S.4    Kras, E.5    Narhi, L.6    Brems, D.7    Gokarn, Y.8
  • 51
    • 77956128486 scopus 로고    scopus 로고
    • Influence of pH on heat-induced aggregation and degradation of therapeutic monoclonal antibodies
    • Ishikawa T, Ito T, Endo R, Nakagawa K, Sawa E, Wakamatsu K. 2010. Influence of pH on heat-induced aggregation and degradation of therapeutic monoclonal antibodies. Biol Pharm Bull 33(8):1413-1417.
    • (2010) Biol Pharm Bull , vol.33 , Issue.8 , pp. 1413-1417
    • Ishikawa, T.1    Ito, T.2    Endo, R.3    Nakagawa, K.4    Sawa, E.5    Wakamatsu, K.6
  • 52
    • 84868584302 scopus 로고    scopus 로고
    • A systematic comparison of free and bound antibodies reveals binding-related conformational changes
    • Sela Culang I, Alon S, Ofran Y. 2012. A systematic comparison of free and bound antibodies reveals binding-related conformational changes. J Immunol 189(10):4890-4899.
    • (2012) J Immunol , vol.189 , Issue.10 , pp. 4890-4899
    • Sela Culang, I.1    Alon, S.2    Ofran, Y.3
  • 53
    • 17944380435 scopus 로고    scopus 로고
    • Crystal structure of a neutralizing human IgG against HIV-1: A template for vaccine design
    • Saphire EO. 2012. Crystal structure of a neutralizing human IgG against HIV-1: A template for vaccine design. Science 293:1155-1158.
    • (2012) Science , vol.293 , pp. 1155-1158
    • Saphire, E.O.1
  • 54
    • 84895920707 scopus 로고    scopus 로고
    • Developability assessment as an early de-risking tool for biopharmaceutical development
    • Zurdo J. 2013. Developability assessment as an early de-risking tool for biopharmaceutical development. Pharm Bioprocess 1(1):29-50.
    • (2013) Pharm Bioprocess , vol.1 , Issue.1 , pp. 29-50
    • Zurdo, J.1


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