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Volumn 9, Issue 4, 2012, Pages 791-802

The influence of charge distribution on self-association and viscosity behavior of monoclonal antibody solutions

Author keywords

electrostatic surface potential; high concentration monoclonal antibody solution; hydrodynamic interaction parameter (H (q)); interaction parameter (k D); membrane confined electrophoresis; protein charge; second virial coefficient (B 22); static structure factor (S (q)); viscosity rheology

Indexed keywords

MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 1; MONOCLONAL ANTIBODY 2; UNCLASSIFIED DRUG;

EID: 84859327683     PISSN: 15438384     EISSN: 15438392     Source Type: Journal    
DOI: 10.1021/mp200566k     Document Type: Article
Times cited : (228)

References (50)
  • 1
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • DOI 10.1002/jps.20079
    • Shire, S. J.; Shahrokh, Z.; Liu, J. Challenges in the development of high protein concentration formulations J. Pharm. Sci. 2004, 93 (6) 1390-1402 (Pubitemid 38725014)
    • (2004) Journal of Pharmaceutical Sciences , vol.93 , Issue.6 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 2
    • 27644477360 scopus 로고    scopus 로고
    • Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution
    • DOI 10.1002/jps.20347
    • Liu, J.; Nguyen, M. D. H.; Andya, J. D.; Shire, S. J. Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution J. Pharm. Sci. 2005, 94 (9) 1928-1940 (Pubitemid 41551477)
    • (2005) Journal of Pharmaceutical Sciences , vol.94 , Issue.9 , pp. 1928-1940
    • Liu, J.1    Nguyen, M.D.H.2    Andya, J.D.3    Shire, S.J.4
  • 4
    • 76649099495 scopus 로고    scopus 로고
    • Specific interactions in high concentration antibody solutions resulting in high viscosity
    • Yadav, S.; Liu, J.; Shire, S. J.; Kalonia, D. S. Specific interactions in high concentration antibody solutions resulting in high viscosity J. Pharm. Sci. 2010, 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
  • 5
    • 79961171856 scopus 로고    scopus 로고
    • Viscosity analysis of high concentration bovine serum albumin aqueous solutions
    • Yadav, S.; Shire, S. J.; Kalonia, D. S. Viscosity analysis of high concentration bovine serum albumin aqueous solutions Pharm. Res. 2011, 28 (8) 1973-1983
    • (2011) Pharm. Res. , vol.28 , Issue.8 , pp. 1973-1983
    • Yadav, S.1    Shire, S.J.2    Kalonia, D.S.3
  • 6
    • 84855891967 scopus 로고    scopus 로고
    • Viscosity behavior of high concentration monoclonal antibody solutions: Correlation with interaction parameter and electroviscous effects
    • Yadav, S.; Shire, S. J.; Kalonia, D. S. Viscosity behavior of high concentration monoclonal antibody solutions: Correlation with interaction parameter and electroviscous effects J. Pharm. Sci. 2012, 101 (3) 998-1011
    • (2012) J. Pharm. Sci. , vol.101 , Issue.3 , pp. 998-1011
    • Yadav, S.1    Shire, S.J.2    Kalonia, D.S.3
  • 7
    • 73949139940 scopus 로고    scopus 로고
    • Understanding and modulating opalescence and viscosity in a monoclonal antibody formulation
    • Salinas, B. A.; Sathish, H. A.; Bishop, S. M.; Harn, N.; Carpenter, J. F.; Randolph, T. W. Understanding and modulating opalescence and viscosity in a monoclonal antibody formulation J. Pharm. Sci. 2009, 99 (1) 82-93
    • (2009) J. Pharm. Sci. , vol.99 , Issue.1 , pp. 82-93
    • Salinas, B.A.1    Sathish, H.A.2    Bishop, S.M.3    Harn, N.4    Carpenter, J.F.5    Randolph, T.W.6
  • 8
    • 55749113694 scopus 로고    scopus 로고
    • Reversible self-association of a concentrated monoclonal antibody solution mediated by Fab-Fab interaction that impacts solution viscosity
    • Kanai, S.; Liu, J.; Patapoff, T. W.; Shire, S. J. Reversible self-association of a concentrated monoclonal antibody solution mediated by Fab-Fab interaction that impacts solution viscosity J. Pharm. Sci. 2008, 97 (10) 4219-4227
    • (2008) J. Pharm. Sci. , vol.97 , Issue.10 , pp. 4219-4227
    • Kanai, S.1    Liu, J.2    Patapoff, T.W.3    Shire, S.J.4
  • 9
    • 78751480205 scopus 로고    scopus 로고
    • Hydrophobic salts markedly diminish viscosity of concentrated protein solutions
    • Du, W.; Klibanov, A. M. Hydrophobic salts markedly diminish viscosity of concentrated protein solutions Biotechnol. Bioeng. 2011, 108 (3) 632-636
    • (2011) Biotechnol. Bioeng. , vol.108 , Issue.3 , pp. 632-636
    • Du, W.1    Klibanov, A.M.2
  • 10
    • 79959866680 scopus 로고    scopus 로고
    • Effect of sugar molecules on the viscosity of high concentration monoclonal antibody solutions
    • He, F.; Woods, C. E.; Litowski, J. R.; Roschen, L. A.; Gadgil, H. S.; Razinkov, V. I.; Kerwin, B. A. Effect of sugar molecules on the viscosity of high concentration monoclonal antibody solutions Pharm. Res. 2011, 28 (7) 1552-1560
    • (2011) Pharm. Res. , vol.28 , Issue.7 , pp. 1552-1560
    • He, F.1    Woods, C.E.2    Litowski, J.R.3    Roschen, L.A.4    Gadgil, H.S.5    Razinkov, V.I.6    Kerwin, B.A.7
  • 12
    • 78049509357 scopus 로고    scopus 로고
    • Factors affecting the viscosity in high concentration solutions of different monoclonal antibodies
    • Yadav, S.; Shire, S. J.; Kalonia, D. S. Factors affecting the viscosity in high concentration solutions of different monoclonal antibodies J. Pharm. Sci. 2010, 99 (12) 4812-4829
    • (2010) J. Pharm. Sci. , vol.99 , Issue.12 , pp. 4812-4829
    • Yadav, S.1    Shire, S.J.2    Kalonia, D.S.3
  • 13
    • 70449112652 scopus 로고    scopus 로고
    • Long- and short-range electrostatic interactions affect the rheology of highly concentrated antibody solutions
    • Chari, R.; Jerath, K.; Badkar, A. V.; Kalonia, D. S. Long- and short-range electrostatic interactions affect the rheology of highly concentrated antibody solutions Pharm. Res. 2009, 26 (12) 2607-2618
    • (2009) Pharm. Res. , vol.26 , Issue.12 , pp. 2607-2618
    • Chari, R.1    Jerath, K.2    Badkar, A.V.3    Kalonia, D.S.4
  • 14
    • 79959871746 scopus 로고    scopus 로고
    • Establishing a link between amino Acid sequences and self-associating and viscoelastic behavior of two closely related monoclonal antibodies
    • Yadav, S.; Sreedhara, A.; Kanai, S.; Liu, J.; Lien, S.; Lowman, H.; Kalonia, D. S.; Shire, S. J. Establishing a link between amino Acid sequences and self-associating and viscoelastic behavior of two closely related monoclonal antibodies Pharm. Res. 2011, 28 (7) 1750-1764
    • (2011) Pharm. Res. , vol.28 , Issue.7 , pp. 1750-1764
    • Yadav, S.1    Sreedhara, A.2    Kanai, S.3    Liu, J.4    Lien, S.5    Lowman, H.6    Kalonia, D.S.7    Shire, S.J.8
  • 15
    • 79952453101 scopus 로고    scopus 로고
    • Use of dynamic light scattering to determine second virial coefficient in a semidilute concentration regime
    • Yadav, S.; Scherer, T. M.; Shire, S. J.; Kalonia, D. S. Use of dynamic light scattering to determine second virial coefficient in a semidilute concentration regime Anal. Biochem. 2011, 411 (2) 292-296
    • (2011) Anal. Biochem. , vol.411 , Issue.2 , pp. 292-296
    • Yadav, S.1    Scherer, T.M.2    Shire, S.J.3    Kalonia, D.S.4
  • 17
    • 0038713535 scopus 로고
    • Effects of intermolecular interaction on protein diffusion in solution
    • Veldkamp, W. B.; Votano, J. R. Effects of intermolecular interaction on protein diffusion in solution J. Phys. Chem. 1976, 80 (25) 2794-2801
    • (1976) J. Phys. Chem. , vol.80 , Issue.25 , pp. 2794-2801
    • Veldkamp, W.B.1    Votano, J.R.2
  • 20
    • 11144267761 scopus 로고    scopus 로고
    • Valence and anion binding of bovine ribonuclease A between pH 6 and 8
    • DOI 10.1016/j.ab.2004.09.009, PII S0003269704007316
    • Moody, T. P.; Kingsbury, J. S.; Durant, J. A.; Wilson, T. J.; Chase, S. F.; Laue, T. M. Valence and anion binding of bovine ribonuclease A between pH 6 and 8 Anal. Biochem. 2005, 336 (2) 243-252 (Pubitemid 40038022)
    • (2005) Analytical Biochemistry , vol.336 , Issue.2 , pp. 243-252
    • Moody, T.P.1    Kingsbury, J.S.2    Durant, J.A.3    Wilson, T.J.4    Chase, S.F.5    Laue, T.M.6
  • 21
    • 0033733114 scopus 로고    scopus 로고
    • A novel interpretation of steady-state electrophoresis experiments
    • Stigter, D. A novel interpretation of steady-state electrophoresis experiments J. Phys. Chem. B 2000, 104 (15) 3402-3404
    • (2000) J. Phys. Chem. B , vol.104 , Issue.15 , pp. 3402-3404
    • Stigter, D.1
  • 22
    • 0011751228 scopus 로고
    • Charge and Potential Distribution at Interface
    • Ottewill, R. H. Rowell, R. L. Academic Press: New York
    • Hunter, R. J., Charge and Potential Distribution at Interface. In Zeta Potential in Colloid Science Principles and Application; Ottewill, R. H.; Rowell, R. L., Eds.; Academic Press: New York, 1981; pp 11-58.
    • (1981) Zeta Potential in Colloid Science Principles and Application , pp. 11-58
    • Hunter, R.J.1
  • 23
    • 0028289241 scopus 로고
    • Anatomy of the antibody molecule
    • DOI 10.1016/0161-5890(94)90001-9
    • Padlan, E. A. Anatomy of the antibody molecule Mol. Immunol. 1994, 31 (3) 169-217 (Pubitemid 24071681)
    • (1994) Molecular Immunology , vol.31 , Issue.3 , pp. 169-217
    • Padlan, E.A.1
  • 27
    • 0000243829 scopus 로고
    • {PROCHECK}: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A.; Macarthur, M. W.; Moss, D. S.; Thornton, J. M. {PROCHECK}: a program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 1993, 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 28
    • 0030870075 scopus 로고    scopus 로고
    • Objectively judging the quality of a protein structure from a Ramachandran plot
    • Hooft, R. W. W.; Sander, C.; Vriend, G. Objectively judging the quality of a protein structure from a Ramachandran plot Comput. Appl. Biosci. 1997, 13 (4) 425-430 (Pubitemid 27384626)
    • (1997) Computer Applications in the Biosciences , vol.13 , Issue.4 , pp. 425-430
    • Hooft, R.W.W.1    Sander, C.2    Vriend, G.3
  • 31
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: Expanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • Dolinsky, T. J.; Czodrowski, P.; Li, H.; Nielsen, J. E.; Jensen, J. H.; Klebe, G.; Baker, N. A. PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations Nucleic Acids Res. 2007, 35 (Web Server issue) W522-W525
    • (2007) Nucleic Acids Res. , vol.35 , Issue.WEB SERVER ISSUE
    • Dolinsky, T.J.1    Czodrowski, P.2    Li, H.3    Nielsen, J.E.4    Jensen, J.H.5    Klebe, G.6    Baker, N.A.7
  • 32
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • Dolinsky, T. J.; Nielsen, J. E.; McCammon, J. A.; Baker, N. A. PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations Nucleic Acids Res. 2004, 32 (Web Server issue) W665-W667
    • (2004) Nucleic Acids Res. , vol.32 , Issue.WEB SERVER ISSUE
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 33
    • 20544435097 scopus 로고    scopus 로고
    • Exploring the helix-coil transition via all-atom equilibrium ensemble simulations
    • DOI 10.1529/biophysj.104.051938
    • Sorin, E. J.; Pande, V. S. Exploring the helix-coil transition via all-atom equilibrium ensemble simulations Biophys. J. 2005, 88 (4) 2472-2493 (Pubitemid 40976118)
    • (2005) Biophysical Journal , vol.88 , Issue.4 , pp. 2472-2493
    • Sorin, E.J.1    Pande, V.S.2
  • 37
    • 0037394496 scopus 로고    scopus 로고
    • Light scattering as a diagnostic for protein crystal growth - A practical approach
    • DOI 10.1016/S1047-8477(03)00038-8
    • Wilson, W. W. Light scattering as a diagnostic for protein crystal growth-A practical approach J. Struct. Biol. 2003, 142 (1) 56-65 (Pubitemid 36457890)
    • (2003) Journal of Structural Biology , vol.142 , Issue.1 , pp. 56-65
    • Wilson, W.W.1
  • 38
    • 79952125250 scopus 로고    scopus 로고
    • Effective charge measurements reveal selective and preferential accumulation of anions, but not cations, at the protein surface in dilute salt solutions
    • Gokarn, Y. R.; Fesinmeyer, R. M.; Saluja, A.; Razinkov, V.; Chase, S. F.; Laue, T. M.; Brems, D. N. Effective charge measurements reveal selective and preferential accumulation of anions, but not cations, at the protein surface in dilute salt solutions Protein Sci. 2011, 20 (3) 580-587
    • (2011) Protein Sci. , vol.20 , Issue.3 , pp. 580-587
    • Gokarn, Y.R.1    Fesinmeyer, R.M.2    Saluja, A.3    Razinkov, V.4    Chase, S.F.5    Laue, T.M.6    Brems, D.N.7
  • 39
    • 79956144642 scopus 로고    scopus 로고
    • A postreductionist framework for protein biochemistry
    • Laue, T.; Demeler, B. A postreductionist framework for protein biochemistry Nat. Chem. Biol. 2011, 7 (6) 331-334
    • (2011) Nat. Chem. Biol. , vol.7 , Issue.6 , pp. 331-334
    • Laue, T.1    Demeler, B.2
  • 40
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • DOI 10.1023/A:1025771421906
    • Chi, E. Y.; Krishnan, S.; Randolph, T. W.; Carpenter, J. F. Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation Pharm. Res. 2003, 20 (9) 1325-1336 (Pubitemid 37164039)
    • (2003) Pharmaceutical Research , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 41
    • 0037378389 scopus 로고    scopus 로고
    • The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient
    • DOI 10.1110/ps.0233703
    • Ho, J. G. S.; Middelberg, A. P. J; Ramage, P.; Kocher, H. P. The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient Protein Sci. 2003, 12 (4) 708-716 (Pubitemid 36348458)
    • (2003) Protein Science , vol.12 , Issue.4 , pp. 708-716
    • Ho, J.G.S.1    Middelberg, A.P.J.2    Ramage, P.3    Kocher, H.P.4
  • 42
    • 0032484699 scopus 로고    scopus 로고
    • Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes
    • DOI 10.1002/(SICI)1097-0290(19980105)57:1<11::AID-BIT2>3.0.CO;2-Y
    • Curtis, R. A.; Prausnitz, J. M.; Blanch, H. W. Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes Biotechnol. Bioeng. 1998, 57 (1) 11-21 (Pubitemid 27514695)
    • (1998) Biotechnology and Bioengineering , vol.57 , Issue.1 , pp. 11-21
    • Curtis, R.A.1    Prausnitz, J.M.2    Blanch, H.W.3
  • 43
    • 0001279457 scopus 로고
    • Predicting protein crystallization from a dilute solution property
    • George, A.; Wilson, W. W. Predicting protein crystallization from a dilute solution property Acta Crystallogr., Sect. D: Biol. Crystallogr. 1994, D50 (4) 361-365
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , Issue.4 , pp. 361-365
    • George, A.1    Wilson, W.W.2
  • 44
    • 0035121714 scopus 로고    scopus 로고
    • Correlation between the osmotic second virial coefficient and the solubility of proteins
    • DOI 10.1021/bp0001314
    • Ruppert, S.; Sandler, S. I.; Lenhoff, A. M. Correlation between the Osmotic Second Virial Coefficient and the Solubility of Proteins Biotechnol. Prog. 2001, 17 (1) 182-187 (Pubitemid 32145390)
    • (2001) Biotechnology Progress , vol.17 , Issue.1 , pp. 182-187
    • Ruppert, S.1    Sandler, S.I.2    Lenhoff, A.M.3
  • 45
    • 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
    • DOI 10.2174/138920105775159313
    • Valente, J. J.; Payne, R. W.; Manning, M. C.; Wilson, W. W.; Henry, C. S. Colloidal Behavior of Proteins: Effects of the Second Virial Coefficient on Solubility, Crystallization and Aggregation of Proteins in Aqueous Solution Curr. Pharm. Biotechnol. 2005, 6 (6) 427-436 (Pubitemid 43137063)
    • (2005) Current Pharmaceutical Biotechnology , 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
  • 47
    • 77953787610 scopus 로고    scopus 로고
    • Observation of a large-scale superstructure in concentrated hemoglobin solutions by using small angle neutron scattering
    • Stadler, A. M.; Schweins, R.; Zaccai, G.; Lindner, P. Observation of a large-scale superstructure in concentrated hemoglobin solutions by using small angle neutron scattering J. Phys. Chem. Lett. 2010, 1 (12) 1805-1808
    • (2010) J. Phys. Chem. Lett. , vol.1 , Issue.12 , pp. 1805-1808
    • Stadler, A.M.1    Schweins, R.2    Zaccai, G.3    Lindner, P.4
  • 48
    • 9644259209 scopus 로고    scopus 로고
    • Equilibrium cluster formation in concentrated protein solutions and colloids
    • DOI 10.1038/nature03109
    • Stradner, A.; Sedgwick, H.; Cardinaux, F.; Poon, W. C. K.; Egelhaaf, S. U.; Schurtenberger, P. Equilibrium cluster formation in concentrated protein solutions and colloids Nature 2004, 432 (7016) 492-495 (Pubitemid 39576527)
    • (2004) Nature , vol.432 , Issue.7016 , pp. 492-495
    • Stradner, A.1    Sedgwick, H.2    Cardinaux, F.3    Poon, W.C.K.4    Egelhaaf, S.U.5    Schurtenberger, P.6
  • 49
    • 0347444949 scopus 로고
    • Dynamics of suspended colloidal spheres
    • Jones, R. B.; Pusey, P. N. Dynamics of suspended colloidal spheres Annu. Rev. Phys. Chem. 1991, 42 (1) 137-169
    • (1991) Annu. Rev. Phys. Chem. , vol.42 , Issue.1 , pp. 137-169
    • Jones, R.B.1    Pusey, P.N.2
  • 50
    • 0029540627 scopus 로고
    • Interactions in undersaturated and supersaturated lysozyme solutions: Static and dynamic light scattering results
    • Muschol, M.; Rosenberger, F. Interactions in undersaturated and supersaturated lysozyme solutions: Static and dynamic light scattering results J. Chem. Phys. 1995, 103 (24) 10424-10432
    • (1995) J. Chem. Phys. , vol.103 , Issue.24 , pp. 10424-10432
    • Muschol, M.1    Rosenberger, F.2


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