메뉴 건너뛰기




Volumn 99, Issue 1, 2010, Pages 82-93

Understanding and modulating opalescence and viscosity in a monoclonal antibody formulation

Author keywords

Light scattering; Physical characterization; Protein delivery; Protein formulation; Viscosity

Indexed keywords

IMMUNOGLOBULIN G1; MONOCLONAL ANTIBODY;

EID: 73949139940     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.21797     Document Type: Article
Times cited : (164)

References (53)
  • 1
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • Shire SJ, Shahrokh Z, Liu J. 2004. Challenges in the development of high protein concentration formulations. J Pharm Sci 93:1390-1402.
    • (2004) J Pharm Sci , vol.93 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 2
    • 0142087554 scopus 로고    scopus 로고
    • Antibodies as therapeutic agents: Vive la renaissance!
    • Stockwin LH, Holmes S. 2003. Antibodies as therapeutic agents: Vive la renaissance! Expert Opin Biol Ther 3:1133-1152.
    • (2003) Expert Opin Biol Ther , vol.3 , pp. 1133-1152
    • Stockwin, L.H.1    Holmes, S.2
  • 3
    • 52449112053 scopus 로고    scopus 로고
    • High concentration formulations of recombinant human interleukin-1 receptor antagonist: II. Aggregation kinetics
    • Alford JR, Kendrick BS, Carpenter JF, Randolph TW. 2008. High concentration formulations of recombinant human interleukin-1 receptor antagonist: II. Aggregation kinetics. J Pharm Sci 97:3005-3021.
    • (2008) J Pharm Sci , vol.97 , pp. 3005-3021
    • Alford, J.R.1    Kendrick, B.S.2    Carpenter, J.F.3    Randolph, T.W.4
  • 4
    • 3242670796 scopus 로고    scopus 로고
    • Opalescent appearance of an IgG1 antibody at high concentrations and its relationship to noncovalent association
    • Sukumar M, Doyle BL, Combs JL, Pekar AH. 2004. Opalescent appearance of an IgG1 antibody at high concentrations and its relationship to noncovalent association. Pharm Res 21:1087-1093.
    • (2004) Pharm Res , vol.21 , pp. 1087-1093
    • Sukumar, M.1    Doyle, B.L.2    Combs, J.L.3    Pekar, A.H.4
  • 5
    • 3843058933 scopus 로고    scopus 로고
    • Commercial manufacturing scale formulation and analytical characterization of therapeutic recombinant antibodies
    • Harris RJ, Shire SJ, Winter C. 2004. Commercial manufacturing scale formulation and analytical characterization of therapeutic recombinant antibodies. Drug Dev Res 61:137-154.
    • (2004) Drug Dev Res , vol.61 , pp. 137-154
    • Harris, R.J.1    Shire, S.J.2    Winter, C.3
  • 6
    • 27644477360 scopus 로고    scopus 로고
    • Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution
    • Liu J, Nquyen MDH, Andya JD, Shire SJ. 2005. Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution. J Pharm Sci 94:1928-1940.
    • (2005) J Pharm Sci , vol.94 , pp. 1928-1940
    • Liu, J.1    Nquyen, M.D.H.2    Andya, J.D.3    Shire, S.J.4
  • 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 TW, Shire SJ. 2008. Reversible self-association of a concentrated monoclonal antibody solution mediated by Fab-Fab interaction that impacts solution viscosity. J Pharm Sci 97: 4219-4227.
    • (2008) J Pharm Sci , vol.97 , pp. 4219-4227
    • Kanai, S.1    Liu, J.2    Patapoff, T.W.3    Shire, S.J.4
  • 9
    • 0034349193 scopus 로고    scopus 로고
    • Protein-protein interactions in aqueous ammonium sulfate solutions. Lysozyme and bovine serum albumin (BSA)
    • Moon YU, Curtis RA, Anderson CO, Blanch HW, Prausnitz JM. 2000. Protein-protein interactions in aqueous ammonium sulfate solutions. Lysozyme and bovine serum albumin (BSA). J Solut Chem 29: 699-717.
    • (2000) J Solut Chem , vol.29 , pp. 699-717
    • Moon, Y.U.1    Curtis, R.A.2    Anderson, C.O.3    Blanch, H.W.4    Prausnitz, J.M.5
  • 10
    • 0032533578 scopus 로고    scopus 로고
    • Understanding nonidealities of the osmotic pressure of concentrated bovine serum albumin
    • Yousef MA, Datta R, Rodgers VGJ. 1998. Understanding nonidealities of the osmotic pressure of concentrated bovine serum albumin. J Colloid Interface Sci 207:273-282.
    • (1998) J Colloid Interface Sci , vol.207 , pp. 273-282
    • Yousef, M.A.1    Datta, R.2    Rodgers, V.G.J.3
  • 11
    • 0028822574 scopus 로고
    • A molecular model for the dependence of the osmotic pressure of bovine serum albumin upon concentration and pH
    • Minton AP. 1995. A molecular model for the dependence of the osmotic pressure of bovine serum albumin upon concentration and pH. Biophys Chem 57:65-70.
    • (1995) Biophys Chem , vol.57 , pp. 65-70
    • Minton, A.P.1
  • 12
    • 38149048416 scopus 로고    scopus 로고
    • The effective hard particle model provides a simple, robust, and broadly applicable description of nonideal behavior in concentrated solutions of bovine serum albumin and other non-associating proteins
    • Minton AP. 2007. The effective hard particle model provides a simple, robust, and broadly applicable description of nonideal behavior in concentrated solutions of bovine serum albumin and other non-associating proteins. J Pharm Sci 96:3466-3469.
    • (2007) J Pharm Sci , vol.96 , pp. 3466-3469
    • Minton, A.P.1
  • 13
    • 41649094226 scopus 로고    scopus 로고
    • Effective hard particle model for the osmotic pressure of highly concentration binary protein solutions
    • Minton AP. 2008. Effective hard particle model for the osmotic pressure of highly concentration binary protein solutions. Biophys J 94:L57-L59.
    • (2008) Biophys J , vol.94
    • Minton, A.P.1
  • 14
    • 0017397771 scopus 로고
    • Hard quasispherical model for the viscosity of hemoglobin solutions
    • Ross PD, Minton AP. 1977. Hard quasispherical model for the viscosity of hemoglobin solutions. Biochem Biophys Res Commun 76:971-976.
    • (1977) Biochem Biophys Res Commun , vol.76 , pp. 971-976
    • Ross, P.D.1    Minton, A.P.2
  • 15
    • 0031829687 scopus 로고    scopus 로고
    • Free-solvent model of osmotic pressure revisited: Application to concentrated IgG solution under physiological conditions
    • Yousef MA, Datta R, Rodgers VGJ. 1998. Free-solvent model of osmotic pressure revisited: Application to concentrated IgG solution under physiological conditions. J Colloid Interface Sci 197: 273-282.
    • (1998) J Colloid Interface Sci , vol.197 , pp. 273-282
    • Yousef, M.A.1    Datta, R.2    Rodgers, V.G.J.3
  • 16
    • 24144467366 scopus 로고    scopus 로고
    • Light-scattering studies of protein solutions: Role of hydration in weak protein-protein interactions
    • Asthagiri D, Paliwal A, Abras D, Lenhoff AM, Paulaitis ME. 2005. Light-scattering studies of protein solutions: Role of hydration in weak protein-protein interactions. Biophys J 89:1564-1573.
    • (2005) Biophys J , vol.89 , pp. 1564-1573
    • Asthagiri, D.1    Paliwal, A.2    Abras, D.3    Lenhoff, A.M.4    Paulaitis, M.E.5
  • 17
    • 33644683427 scopus 로고    scopus 로고
    • Negative second virial coefficients as predictors of protein crystal growth: Evidence from sedimentation equilibrium studies that refutes the designation of those light scattering parameters as osmotic virial coefficients
    • Deszczynski M, Harding SE, Winzor DJ. 2006. Negative second virial coefficients as predictors of protein crystal growth: Evidence from sedimentation equilibrium studies that refutes the designation of those light scattering parameters as osmotic virial coefficients. Biophys Chem 120:106-113.
    • (2006) Biophys Chem , vol.120 , pp. 106-113
    • Deszczynski, M.1    Harding, S.E.2    Winzor, D.J.3
  • 18
    • 0000953383 scopus 로고    scopus 로고
    • Using the phase transitions to investigate the effect of salts on protein interactions
    • Broide ML, Tominc TM, Saxowsky MD. 1996. Using the phase transitions to investigate the effect of salts on protein interactions. Phys Rev E 53: 6325-6335.
    • (1996) Phys Rev E , vol.53 , pp. 6325-6335
    • Broide, M.L.1    Tominc, T.M.2    Saxowsky, M.D.3
  • 19
    • 4644351191 scopus 로고    scopus 로고
    • Determination of protein charge by capillary zone electrophoresis
    • Winzor DJ, Jones S, Harding SE. 2004. Determination of protein charge by capillary zone electrophoresis. Anal Biochem 333:225-229.
    • (2004) Anal Biochem , vol.333 , pp. 225-229
    • Winzor, D.J.1    Jones, S.2    Harding, S.E.3
  • 20
    • 0347989358 scopus 로고    scopus 로고
    • Determination of the net charge (valence) of a protein: A fundamental but elusive parameter
    • Winzor DJ. 2004. Determination of the net charge (valence) of a protein: A fundamental but elusive parameter. Anal Biochem 325:1-20.
    • (2004) Anal Biochem , vol.325 , pp. 1-20
    • Winzor, D.J.1
  • 21
    • 17644443266 scopus 로고    scopus 로고
    • Use of T4 lysozyme charge mutants to examine electrophoretic models
    • Durant JA, Chen C, Laue TM, Moody TP, Allison SA. 2002. Use of T4 lysozyme charge mutants to examine electrophoretic models. Biophys Chem 101-102:593-609.
    • (2002) Biophys Chem , vol.101-102 , pp. 593-609
    • Durant, J.A.1    Chen, C.2    Laue, T.M.3    Moody, T.P.4    Allison, S.A.5
  • 22
    • 34447638512 scopus 로고    scopus 로고
    • Fast determination of conditions for maximum dynamic capacity in cation-exchange chromatography of human monoclonal antibodies
    • Faude A, Zacher D, Müller E, Böttinger H. 2007. Fast determination of conditions for maximum dynamic capacity in cation-exchange chromatography of human monoclonal antibodies. J Chromatogr A 1161:29-35.
    • (2007) J Chromatogr A , vol.1161 , pp. 29-35
    • Faude, A.1    Zacher, D.2    Müller, E.3    Böttinger, H.4
  • 24
    • 34249290252 scopus 로고
    • The viscosity of a concentrated suspension of spherical particles
    • Mooney M. 1951. The viscosity of a concentrated suspension of spherical particles. J Colloid Sci 6: 162-170.
    • (1951) J Colloid Sci , vol.6 , pp. 162-170
    • Mooney, M.1
  • 25
    • 0034737923 scopus 로고    scopus 로고
    • Viscosity analysis of the temperature dependence of the solution conformation of ovalbumin
    • Monkos K. 2000. Viscosity analysis of the temperature dependence of the solution conformation of ovalbumin. Biophys Chem 85:7-16.
    • (2000) Biophys Chem , vol.85 , pp. 7-16
    • Monkos, K.1
  • 26
    • 7144264367 scopus 로고
    • The viscosity of dilute solutions of long-chain molecules. IV. Dependence on concentration
    • Huggins ML. 1942. The viscosity of dilute solutions of long-chain molecules. IV. Dependence on concentration. J Am Chem Soc 64:2716-2718.
    • (1942) J Am Chem Soc , vol.64 , pp. 2716-2718
    • Huggins, M.L.1
  • 28
    • 0001117617 scopus 로고
    • Equation of state for nonattracting rigid spheres
    • Carnahan NF, Starling KE. 1969. Equation of state for nonattracting rigid spheres. J Chem Phys 51: 635-636.
    • (1969) J Chem Phys , vol.51 , pp. 635-636
    • Carnahan, N.F.1    Starling, K.E.2
  • 30
    • 0035894369 scopus 로고    scopus 로고
    • Determination of carbohydrate contents from excess light scattering
    • Arakawa T, Wen J. 2001. Determination of carbohydrate contents from excess light scattering. Anal Biochem 299:158-161.
    • (2001) Anal Biochem , vol.299 , pp. 158-161
    • Arakawa, T.1    Wen, J.2
  • 31
    • 40649121245 scopus 로고    scopus 로고
    • Rigorous estimation of effective protein charge from experimental electrophoretic mobilities for proteomics analysis using microchip electrophoresis
    • Chun M, Lee I. 2008. Rigorous estimation of effective protein charge from experimental electrophoretic mobilities for proteomics analysis using microchip electrophoresis. Colloids Surf A 318:191-198.
    • (2008) Colloids Surf A , vol.318 , pp. 191-198
    • Chun, M.1    Lee, I.2
  • 32
    • 0031554728 scopus 로고    scopus 로고
    • The intrinsic viscosity of biological macromolecules. Progress in measurement, interpretation and application to structure in dilute solution
    • Harding SE. 1997. The intrinsic viscosity of biological macromolecules. Progress in measurement, interpretation and application to structure in dilute solution. Prog Biophys Mol Biol 68:207-262.
    • (1997) Prog Biophys Mol Biol , vol.68 , pp. 207-262
    • Harding, S.E.1
  • 33
    • 33748937041 scopus 로고    scopus 로고
    • Application of high-frequency rheology measurements for analyzing protein - protein interactions in high protein concentration solutions using a model monoclonal antibody (IgG2)
    • Saluja A, Badkar AV, Zeng DL, Nema S, Kalonia DS. 2004. Application of high-frequency rheology measurements for analyzing protein - protein interactions in high protein concentration solutions using a model monoclonal antibody (IgG2). J Pharm Sci 95:1967-1983.
    • (2004) J Pharm Sci , vol.95 , pp. 1967-1983
    • Saluja, A.1    Badkar, A.V.2    Zeng, D.L.3    Nema, S.4    Kalonia, D.S.5
  • 34
    • 84974626611 scopus 로고
    • Molecular kinetic theory of opalescence of gases in their critical region and of some allied phenomenon
    • Smoluchowski M. 1908. Molecular kinetic theory of opalescence of gases in their critical region and of some allied phenomenon. Ann Phys 25:205-226.
    • (1908) Ann Phys , vol.25 , pp. 205-226
    • Smoluchowski, M.1
  • 35
    • 84952787536 scopus 로고
    • Theory of the opalescence of homogeneous and of mixed liquids in the neighborhood of the critical region
    • Einstein A. 1910. Theory of the opalescence of homogeneous and of mixed liquids in the neighborhood of the critical region. Ann Phys 33:1275-1298.
    • (1910) Ann Phys , vol.33 , pp. 1275-1298
    • Einstein, A.1
  • 36
    • 0001372987 scopus 로고
    • Critical opalescence of polystyrene in cyclohexane: Range of molecular forces and radius of gyration
    • Debye P, Chu B, Woermann D. 1962. Critical opalescence of polystyrene in cyclohexane: Range of molecular forces and radius of gyration. J Chem Phys 36:1803-1808.
    • (1962) J Chem Phys , vol.36 , pp. 1803-1808
    • Debye, P.1    Chu, B.2    Woermann, D.3
  • 37
    • 0001631379 scopus 로고
    • Critical opalescence of macromolecular solutions
    • de Gennes PG. 1968. Critical opalescence of macromolecular solutions. Phys Lett 26A:313-314.
    • (1968) Phys Lett , vol.26 A , pp. 313-314
    • de Gennes, P.G.1
  • 38
    • 0009415509 scopus 로고
    • Comments of critical opalescence of macromolecular solutions
    • Chu B. 1969. Comments of critical opalescence of macromolecular solutions. Phys Lett 28A:654-655.
    • (1969) Phys Lett , vol.28 A , pp. 654-655
    • Chu, B.1
  • 40
    • 0001118365 scopus 로고
    • Critical behavior of a binary mixture of protein and salt water
    • Ishimoto C, Tanaka T. 1977. Critical behavior of a binary mixture of protein and salt water. Phys Rev Lett 39:474-477.
    • (1977) Phys Rev Lett , vol.39 , pp. 474-477
    • Ishimoto, C.1    Tanaka, T.2
  • 43
    • 73949150477 scopus 로고
    • Critical opalescence and the macromolecule
    • Chu B. 1970. Critical opalescence and the macromolecule. Adv Macromol Chem 2:89-120.
    • (1970) Adv Macromol Chem , vol.2 , pp. 89-120
    • Chu, B.1
  • 44
    • 4143063021 scopus 로고    scopus 로고
    • Thermodynamic instability in supersaturated lysozyme solutions: Effect of salt and role of concentration fluctuations
    • Manno M, Xiao C, Bulone D, Martorana V, San Biagio PL. 2003. Thermodynamic instability in supersaturated lysozyme solutions: Effect of salt and role of concentration fluctuations. Phys Rev E 68:011904-1-011904-11.
    • (2003) Phys Rev E , vol.68
    • Manno, M.1    Xiao, C.2    Bulone, D.3    Martorana, V.4    San Biagio, P.L.5
  • 45
    • 33644694594 scopus 로고    scopus 로고
    • Light scattering and phase behavior of lysozyme-poly(ethylene glycol) mixtures
    • Bloustine J, Virmani T, Thurston GM, Fraden S. 2006. Light scattering and phase behavior of lysozyme-poly(ethylene glycol) mixtures. Phys Rev Lett 96:087803-1-087803-4.
    • (2006) Phys Rev Lett , vol.96
    • Bloustine, J.1    Virmani, T.2    Thurston, G.M.3    Fraden, S.4
  • 46
    • 0001279457 scopus 로고
    • Predicting protein crystallization from a dilute solution property
    • George A, Wilson WW. 1994. Predicting protein crystallization from a dilute solution property. Acta Crystallogr D50:361-365.
    • (1994) Acta Crystallogr , vol.D50 , pp. 361-365
    • George, A.1    Wilson, W.W.2
  • 47
    • 0036795672 scopus 로고    scopus 로고
    • Correlation between the osmotic second virial coefficient and solubility for equine serum albumin and ovalbumin
    • Demoruelle K, Guo B, Kao S, McDonald MM, Nikic DB, Holman SC, Wilson WW. 2002. Correlation between the osmotic second virial coefficient and solubility for equine serum albumin and ovalbumin. Acta Crystallogr D58:1544-1548.
    • (2002) Acta Crystallogr , vol.D58 , pp. 1544-1548
    • Demoruelle, K.1    Guo, B.2    Kao, S.3    McDonald, M.M.4    Nikic, D.B.5    Holman, S.C.6    Wilson, W.W.7
  • 48
    • 38349042010 scopus 로고    scopus 로고
    • Protein phase behavior in aqueous solutions: Crystallization, liquid-liquid phase separation, gels and aggregates
    • Dumetz AC, Chockla AM, Kaler EW, Lenhoff AM. 2008. Protein phase behavior in aqueous solutions: Crystallization, liquid-liquid phase separation, gels and aggregates. Biophys J 94:570-583.
    • (2008) Biophys J , vol.94 , pp. 570-583
    • Dumetz, A.C.1    Chockla, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 49
    • 0037195131 scopus 로고    scopus 로고
    • Effect of polyethylene glycol on the liquid - liquid phase transition in aqueous protein solutions
    • Annunziata O, Asherie N, Lomakin A, Pande J, Ogun O, Benedek GB. 2002. Effect of polyethylene glycol on the liquid - liquid phase transition in aqueous protein solutions. Proc Natl Acad Sci USA 99:14165-14170.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14165-14170
    • Annunziata, O.1    Asherie, N.2    Lomakin, A.3    Pande, J.4    Ogun, O.5    Benedek, G.B.6
  • 51
    • 0346331223 scopus 로고    scopus 로고
    • Cloud and solubility temperatures versus ionic strength in model lysozyme solutions
    • Pellicane G, Costa D, Caccamo C. 2003. Cloud and solubility temperatures versus ionic strength in model lysozyme solutions. J Phys Condens Matter 15:S3485-S3489.
    • (2003) J Phys Condens Matter , vol.15
    • Pellicane, G.1    Costa, D.2    Caccamo, C.3
  • 52
    • 0031175651 scopus 로고    scopus 로고
    • Lysozyme-lysozyme interactions in under- and super-saturated solutions: A simple relation between the second virial coefficients in H20 and D20
    • Gripon C, Legrand L, Rosenman I, Vidal O, Robert MC, Boub F. 1997. Lysozyme-lysozyme interactions in under- and super-saturated solutions: A simple relation between the second virial coefficients in H20 and D20. J Cryst Growth 178:575-584.
    • (1997) J Cryst Growth , vol.178 , pp. 575-584
    • Gripon, C.1    Legrand, L.2    Rosenman, I.3    Vidal, O.4    Robert, M.C.5    Boub, F.6
  • 53
    • 0037471748 scopus 로고    scopus 로고
    • Phase coexistence in a DLVO model of globular protein solutions
    • Pellicane G, Costa D, Caccamo C. 2003. Phase coexistence in a DLVO model of globular protein solutions. J Phys Condens Matter 15:375-384.
    • (2003) J Phys Condens Matter , vol.15 , pp. 375-384
    • Pellicane, G.1    Costa, D.2    Caccamo, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.