메뉴 건너뛰기




Volumn 11, Issue 5, 2014, Pages 1391-1402

Quantitative evaluation of colloidal stability of antibody solutions using PEG-induced liquid-liquid phase separation

Author keywords

antibody; binding energy; colloidal stability; liquid liquid phase separation; PEG

Indexed keywords

IMMUNOGLOBULIN G; MACROGOL; MONOCLONAL ANTIBODY; PROTEIN; ANTIBODY; COLLOID; MACROGOL DERIVATIVE; SOLUTION AND SOLUBILITY;

EID: 84899858498     PISSN: 15438384     EISSN: 15438392     Source Type: Journal    
DOI: 10.1021/mp400521b     Document Type: Article
Times cited : (64)

References (42)
  • 2
    • 77952684807 scopus 로고    scopus 로고
    • The use of native cation-exchange chromatography to study aggregation and phase separation of monoclonal antibodies
    • Chen, S.; Lau, H.; Brodsky, Y.; Kleemann, G. R.; Latypov, R. F. The use of native cation-exchange chromatography to study aggregation and phase separation of monoclonal antibodies Protein Sci. 2010, 19, 1191-1204
    • (2010) Protein Sci. , vol.19 , pp. 1191-1204
    • Chen, S.1    Lau, H.2    Brodsky, Y.3    Kleemann, G.R.4    Latypov, R.F.5
  • 3
    • 77953617541 scopus 로고    scopus 로고
    • Phase separation of an IgG1 antibody solution under a low ionic strength condition
    • Nishi, H.; Miyajima, M.; Nakagami, H.; Noda, M.; Uchiyama, S.; Fukui, K. Phase separation of an IgG1 antibody solution under a low ionic strength condition Pharm. Res. 2010, 27, 1348-1360
    • (2010) Pharm. Res. , vol.27 , pp. 1348-1360
    • Nishi, H.1    Miyajima, M.2    Nakagami, H.3    Noda, M.4    Uchiyama, S.5    Fukui, K.6
  • 4
    • 78649892101 scopus 로고    scopus 로고
    • Liquid-liquid phase separation of a monoclonal antibody and nonmonotonic influence of Hofmeister anions
    • Mason, B. D.; Zhang-van Enk, J.; Zhang, L.; Remmele, R. L., Jr.; Zhang, J. Liquid-liquid phase separation of a monoclonal antibody and nonmonotonic influence of Hofmeister anions Biophys. J. 2010, 99, 3792-3800
    • (2010) Biophys. J. , vol.99 , pp. 3792-3800
    • Mason, B.D.1    Zhang-Van Enk, J.2    Zhang, L.3    Remmele Jr., R.L.4    Zhang, J.5
  • 5
    • 80053630809 scopus 로고    scopus 로고
    • Phase separation in solutions of monoclonal antibodies and the effect of human serum albumin
    • Wang, Y.; Lomakin, A.; Latypov, R. F.; Benedek, G. B. Phase separation in solutions of monoclonal antibodies and the effect of human serum albumin Proc. Natl. Acad. Sci. U.S.A. 2011, 108, 16606-16611
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 16606-16611
    • Wang, Y.1    Lomakin, A.2    Latypov, R.F.3    Benedek, G.B.4
  • 6
    • 79961027385 scopus 로고    scopus 로고
    • Crystallization and liquid-liquid phase separation of monoclonal antibodies and fc-fusion proteins: Screening results
    • Trilisky, E.; Gillespie, R.; Osslund, T. D.; Vunnum, S. Crystallization and liquid-liquid phase separation of monoclonal antibodies and fc-fusion proteins: Screening results Biotechnol. Prog. 2011, 27 (4) 1054-1067
    • (2011) Biotechnol. Prog. , vol.27 , Issue.4 , pp. 1054-1067
    • Trilisky, E.1    Gillespie, R.2    Osslund, T.D.3    Vunnum, S.4
  • 7
    • 80053232304 scopus 로고    scopus 로고
    • Opalescence of an IgG2 monoclonal antibody solution as it relates to liquid-liquid phase separation
    • Mason, B. D.; Zhang, L.; Remmele, R. L., Jr.; Zhang, J. Opalescence of an IgG2 monoclonal antibody solution as it relates to liquid-liquid phase separation J. Pharm. Sci. 2011, 100, 4587-4596
    • (2011) J. Pharm. Sci. , vol.100 , pp. 4587-4596
    • Mason, B.D.1    Zhang, L.2    Remmele Jr., R.L.3    Zhang, J.4
  • 9
    • 84862876623 scopus 로고    scopus 로고
    • Native-state solubility and transfer free energy as predictive tools for selecting excipients to include in protein formulation development studies
    • Banks, D. D.; Latypov, R. F.; Ketchem, R. R.; Woodard, J.; Scavezze, J. L.; Siska, C. C.; Razinkov, V. I. Native-state solubility and transfer free energy as predictive tools for selecting excipients to include in protein formulation development studies J. Pharm. Sci. 2012, 101, 2720-2732
    • (2012) J. Pharm. Sci. , vol.101 , pp. 2720-2732
    • Banks, D.D.1    Latypov, R.F.2    Ketchem, R.R.3    Woodard, J.4    Scavezze, J.L.5    Siska, C.C.6    Razinkov, V.I.7
  • 10
    • 84881026589 scopus 로고    scopus 로고
    • Application of a kosmotrope-based solubility assay to multiple protein therapeutic classes indicates broad use as a high-throughput screen for protein therapeutic aggregation propensity
    • Yamniuk, A. P.; Ditto, N.; Patel, M.; Dai, J.; Sejwal, P.; Stetsko, P.; Doyle, M. L. Application of a kosmotrope-based solubility assay to multiple protein therapeutic classes indicates broad use as a high-throughput screen for protein therapeutic aggregation propensity J. Pharm. Sci. 2013, 102 (8) 2424-2439
    • (2013) J. Pharm. Sci. , vol.102 , Issue.8 , pp. 2424-2439
    • Yamniuk, A.P.1    Ditto, N.2    Patel, M.3    Dai, J.4    Sejwal, P.5    Stetsko, P.6    Doyle, M.L.7
  • 11
    • 79251581274 scopus 로고    scopus 로고
    • Application of a high-throughput screening procedure with PEG-induced precipitation to compare relative protein solubility during formulation development with IgG1 monoclonal antibodies
    • Gibson, T. J.; McCarty, K.; McFadyen, I. J.; Cash, E.; Dalmonte, P.; Hinds, K. D.; Dinerman, A. A.; Alvarez, J. C.; Volkin, D. B. Application of a high-throughput screening procedure with PEG-induced precipitation to compare relative protein solubility during formulation development with IgG1 monoclonal antibodies J. Pharm. Sci. 2011, 100, 1009-1021
    • (2011) J. Pharm. Sci. , vol.100 , pp. 1009-1021
    • Gibson, T.J.1    McCarty, K.2    McFadyen, I.J.3    Cash, E.4    Dalmonte, P.5    Hinds, K.D.6    Dinerman, A.A.7    Alvarez, J.C.8    Volkin, D.B.9
  • 13
    • 0027085826 scopus 로고
    • Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols
    • Bhat, R.; Timasheff, S. N. Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols Protein Sci. 1992, 1, 1133-1143
    • (1992) Protein Sci. , vol.1 , pp. 1133-1143
    • Bhat, R.1    Timasheff, S.N.2
  • 15
    • 84855877977 scopus 로고    scopus 로고
    • Formulation design and high-throughput excipient selection based on structural integrity and conformational stability of dilute and highly concentrated IgG1 monoclonal antibody solutions
    • Bhambhani, A.; Kissmann, J. M.; Joshi, S. B.; Volkin, D. B.; Kashi, R. S.; Middaugh, C. R. Formulation design and high-throughput excipient selection based on structural integrity and conformational stability of dilute and highly concentrated IgG1 monoclonal antibody solutions J. Pharm. Sci. 2012, 101, 1120-1135
    • (2012) J. Pharm. Sci. , vol.101 , pp. 1120-1135
    • Bhambhani, A.1    Kissmann, J.M.2    Joshi, S.B.3    Volkin, D.B.4    Kashi, R.S.5    Middaugh, C.R.6
  • 17
    • 33751552849 scopus 로고
    • Liquid-liquid phase separation of aqueous lysozyme solutions: Effects of pH and salt identity
    • Taratuta, V. G.; Holschbach, A.; Thurston, G. M.; Blankschtein, D.; Benedek, G. B. Liquid-liquid phase separation of aqueous lysozyme solutions: effects of pH and salt identity J. Phys. Chem. 1990, 94, 2140-2144
    • (1990) J. Phys. Chem. , vol.94 , pp. 2140-2144
    • Taratuta, V.G.1    Holschbach, A.2    Thurston, G.M.3    Blankschtein, D.4    Benedek, G.B.5
  • 19
    • 38349042010 scopus 로고    scopus 로고
    • Protein phase behavior in aqueous solutions: Crystallization, liquid-liquid phase separation, gels, and aggregates
    • Dumetz, A. C.; Chockla, A. M.; Kaler, E. W.; Lenhoff, A. M. Protein phase behavior in aqueous solutions: crystallization, liquid-liquid phase separation, gels, and aggregates Biophys. J. 2008, 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
  • 22
    • 0037417980 scopus 로고    scopus 로고
    • Observation of liquid-liquid phase separation for eye lens gammaS-Crystallin
    • Annunziata, O.; Ogun, O.; Benedek, G. B. Observation of liquid-liquid phase separation for eye lens gammaS-Crystallin Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 970-974
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 970-974
    • Annunziata, O.1    Ogun, O.2    Benedek, G.B.3
  • 23
    • 8344281751 scopus 로고    scopus 로고
    • Monte Carlo study of phase separation in aqueous protein solutions
    • Lomakin, A.; Asherie, N.; Benedek, G. B. Monte Carlo study of phase separation in aqueous protein solutions J. Chem. Phys. 1996, 104, 1646-1656
    • (1996) J. Chem. Phys. , vol.104 , pp. 1646-1656
    • Lomakin, A.1    Asherie, N.2    Benedek, G.B.3
  • 24
    • 42149114445 scopus 로고    scopus 로고
    • Liquid-liquid phase transition of protein aqueous solutions isothermally induced by protein cross-linking
    • Wang, Y.; Annunziata, O. Liquid-liquid phase transition of protein aqueous solutions isothermally induced by protein cross-linking Langmuir 2008, 24, 2799-2807
    • (2008) Langmuir , vol.24 , pp. 2799-2807
    • Wang, Y.1    Annunziata, O.2
  • 25
    • 16444382474 scopus 로고
    • Phase behaviour of concentrated suspensions of nearly hard colloidal spheres
    • Pusey, P. N.; van Megen, W. Phase behaviour of concentrated suspensions of nearly hard colloidal spheres Nature 1986, 320, 340-342
    • (1986) Nature , vol.320 , pp. 340-342
    • Pusey, P.N.1    Van Megen, W.2
  • 26
    • 0000508062 scopus 로고
    • Phase transitions in systems with extremely short-ranged attractions: A density-functional theory
    • Rascón, C.; Navascués, G.; Mederos, L. Phase transitions in systems with extremely short-ranged attractions: A density-functional theory Phys. Rev. B 1995, 51, 14899-14906
    • (1995) Phys. Rev. B , vol.51 , pp. 14899-14906
    • Rascón, C.1    Navascués, G.2    Mederos, L.3
  • 27
    • 0031559476 scopus 로고    scopus 로고
    • Liquid-liquid phase separation in supersaturated lysozyme solutions and associated precipitate formation/crystallization
    • Muschol, M.; Rosenberger, F. Liquid-liquid phase separation in supersaturated lysozyme solutions and associated precipitate formation/crystallization J. Chem. Phys. 1997, 107, 1953-1962
    • (1997) J. Chem. Phys. , vol.107 , pp. 1953-1962
    • Muschol, M.1    Rosenberger, F.2
  • 30
    • 0035942984 scopus 로고    scopus 로고
    • Cloud-point temperatures for lysozyme in electrolyte solutions: Effect of salt type, salt concentration and pH
    • Grigsby, J. J.; Blanch, H. W.; Prausnitz, J. M. Cloud-point temperatures for lysozyme in electrolyte solutions: effect of salt type, salt concentration and pH Biophys. Chem. 2001, 91, 231-243
    • (2001) Biophys. Chem. , vol.91 , pp. 231-243
    • Grigsby, J.J.1    Blanch, H.W.2    Prausnitz, J.M.3
  • 32
    • 34250642327 scopus 로고    scopus 로고
    • Modifications of therapeutic proteins: Challenges and prospects
    • Jenkins, N. Modifications of therapeutic proteins: challenges and prospects Cytotechnology 2007, 53, 121-125
    • (2007) Cytotechnology , vol.53 , pp. 121-125
    • Jenkins, N.1
  • 33
    • 79960135244 scopus 로고    scopus 로고
    • Chemical modifications in therapeutic protein aggregates generated under different stress conditions
    • Luo, Q.; Joubert, M. K.; Stevenson, R.; Ketchem, R. R.; Narhi, L. O.; Wypych, J. Chemical modifications in therapeutic protein aggregates generated under different stress conditions J. Biol. Chem. 2011, 286, 25134-25144
    • (2011) J. Biol. Chem. , vol.286 , pp. 25134-25144
    • Luo, Q.1    Joubert, M.K.2    Stevenson, R.3    Ketchem, R.R.4    Narhi, L.O.5    Wypych, J.6
  • 34
    • 0028985146 scopus 로고
    • Oxidation of gamma II-Crystallin solutions yields dimers with a high phase separation temperature
    • Pande, J.; Lomakin, A.; Fine, B.; Ogun, O.; Sokolinski, I.; Benedek, G. Oxidation of gamma II-Crystallin solutions yields dimers with a high phase separation temperature Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 1067-1071
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1067-1071
    • Pande, J.1    Lomakin, A.2    Fine, B.3    Ogun, O.4    Sokolinski, I.5    Benedek, G.6
  • 35
    • 13444306217 scopus 로고    scopus 로고
    • Oligomerization and phase transitions in aqueous solutions of native and truncated human beta B1-Crystallin
    • Annunziata, O.; Pande, A.; Pande, J.; Ogun, O.; Lubsen, N. H.; Benedek, G. B. Oligomerization and phase transitions in aqueous solutions of native and truncated human beta B1-Crystallin Biochemistry 2005, 44, 1316-1328
    • (2005) Biochemistry , vol.44 , pp. 1316-1328
    • Annunziata, O.1    Pande, A.2    Pande, J.3    Ogun, O.4    Lubsen, N.H.5    Benedek, G.B.6
  • 37
    • 33847078030 scopus 로고    scopus 로고
    • Comparison between protein-polyethylene glycol (PEG) interactions and the effect of PEG on protein-protein interactions using the liquid-liquid phase transition
    • Wang, Y.; Annunziata, O. Comparison between protein-polyethylene glycol (PEG) interactions and the effect of PEG on protein-protein interactions using the liquid-liquid phase transition J. Phys. Chem. B 2007, 111, 1222-1230
    • (2007) J. Phys. Chem. B , vol.111 , pp. 1222-1230
    • Wang, Y.1    Annunziata, O.2
  • 38
    • 0036769001 scopus 로고    scopus 로고
    • Catching the PEG-induced attractive interaction between proteins
    • Vivares, D.; Belloni, L.; Tardieu, A.; Bonneté, F. Catching the PEG-induced attractive interaction between proteins Eur. Phys. J. E 2002, 9, 15-25
    • (2002) Eur. Phys. J. e , vol.9 , pp. 15-25
    • Vivares, D.1    Belloni, L.2    Tardieu, A.3    Bonneté, F.4
  • 39
    • 0022381773 scopus 로고
    • Mechanism of poly(ethylene glycol) interaction with proteins
    • Arakawa, T.; Timasheff, S. N. Mechanism of poly(ethylene glycol) interaction with proteins Biochemistry 1985, 24, 6756-6762
    • (1985) Biochemistry , vol.24 , pp. 6756-6762
    • Arakawa, T.1    Timasheff, S.N.2
  • 41
    • 65249084081 scopus 로고    scopus 로고
    • A phenomenological one-parameter equation of state for osmotic pressures of PEG and other neutral flexible polymers in good solvents
    • Cohen, J. A.; Podgornik, R.; Hansen, P. L.; Parsegian, V. A. A phenomenological one-parameter equation of state for osmotic pressures of PEG and other neutral flexible polymers in good solvents J. Phys. Chem. B 2009, 113, 3709-3714
    • (2009) J. Phys. Chem. B , vol.113 , pp. 3709-3714
    • Cohen, J.A.1    Podgornik, R.2    Hansen, P.L.3    Parsegian, V.A.4
  • 42
    • 33644694594 scopus 로고    scopus 로고
    • Light scattering and phase behavior of lysozyme-poly(ethylene glycol) mixtures
    • Bloustine, J.; Virmani, T.; Thurston, G. M.; Fraden, S. Light scattering and phase behavior of lysozyme-poly(ethylene glycol) mixtures Phys. Rev. Lett. 2006, 96, 087803
    • (2006) Phys. Rev. Lett. , vol.96 , pp. 087803
    • Bloustine, J.1    Virmani, T.2    Thurston, G.M.3    Fraden, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.