메뉴 건너뛰기




Volumn 13, Issue 8, 2015, Pages

Development of a high-throughput formulation screening platform for monoclonal antibodies

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; AMMONIUM ACETATE; AMMONIUM SULFATE; CITRATE SODIUM; DODECYL SULFATE SODIUM; HISTIDINE; IMIDAZOLE; IMMUNOGLOBULIN G1 ANTIBODY; SODIUM CHLORIDE; SODIUM DIHYDROGEN PHOSPHATE; SUCCINIC ACID;

EID: 84946593929     PISSN: 15426319     EISSN: None     Source Type: Trade Journal    
DOI: None     Document Type: Article
Times cited : (4)

References (33)
  • 1
    • 52449112071 scopus 로고    scopus 로고
    • Heterogeneity of monoclonal antibodies
    • Liu H, et al. Heterogeneity of Monoclonal Antibodies. J. Pharm. Sci. 97(7) 2008: 2426-2447.
    • (2008) J. Pharm. Sci. , vol.97 , Issue.7 , pp. 2426-2447
    • Liu, H.1
  • 2
    • 12844278044 scopus 로고    scopus 로고
    • The oxidative environment and protein damage
    • Davies MJ. The Oxidative Environment and Protein Damage. Biochim. Biophys. Acta. 1703(2) 2005: 93-109.
    • (2005) Biochim. Biophys. Acta. , vol.1703 , Issue.2 , pp. 93-109
    • Davies, M.J.1
  • 3
    • 34548040973 scopus 로고    scopus 로고
    • Analysis of post-translational modifications in recombinant monoclonal antibody igg1 by reversed-phase liquid chromatography/mass spectrometry
    • Yan B, et al. Analysis of Post-Translational Modifications in Recombinant Monoclonal Antibody IgG1 By Reversed-Phase Liquid Chromatography/Mass Spectrometry. J. Chromatogr. A 1164(1-2) 2007: 153-161.
    • (2007) J. Chromatogr. A , vol.1164 , Issue.1-2 , pp. 153-161
    • Yan, B.1
  • 4
    • 79960135244 scopus 로고    scopus 로고
    • Chemical modifications in therapeutic protein aggregates generated under different stress conditions
    • Luo Q, et al. Chemical Modifications in Therapeutic Protein Aggregates Generated Under Different Stress Conditions. J. Biol. Chem. 286(28) 2011: 25134-25144.
    • (2011) J. Biol. Chem. , vol.286 , Issue.28 , pp. 25134-25144
    • Luo, Q.1
  • 5
    • 84896514767 scopus 로고    scopus 로고
    • Assessment of chemical modifications of sites in the cdrs of recombinant antibodies: Susceptibility vs. Functionality of critical quality attributes
    • Haberger M, et al. Assessment of Chemical Modifications of Sites in the CDRs of Recombinant Antibodies: Susceptibility vs. Functionality of Critical Quality Attributes. MAbs 6(2) 2014: 327-339.
    • (2014) MAbs , vol.6 , Issue.2 , pp. 327-339
    • Haberger, M.1
  • 6
    • 70349229289 scopus 로고    scopus 로고
    • Succinimide formation at asn 55 in the complementarity determining region of a recombinant monoclonal antibody igg1 heavy chain
    • Yan B, et al. Succinimide Formation at Asn 55 in the Complementarity Determining Region of a Recombinant Monoclonal Antibody IgG1 Heavy Chain. J. Pharm. Sci. 98(10) 2009: 3509-3521.
    • (2009) J. Pharm. Sci. , vol.98 , Issue.10 , pp. 3509-3521
    • Yan, B.1
  • 7
    • 80052270546 scopus 로고    scopus 로고
    • Predicting accelerated aggregation rates for monoclonal antibody formulations, and challenges for low-temperature predictions
    • Brummitt RK, Nesta DP, Roberts CJ. Predicting Accelerated Aggregation Rates for Monoclonal Antibody Formulations, and Challenges for Low-Temperature Predictions. J. Pharm. Sci. 100(10) 2011: 4234-4243.
    • (2011) J. Pharm. Sci. , vol.100 , Issue.10 , pp. 4234-4243
    • Brummitt, R.K.1    Nesta, D.P.2    Roberts, C.J.3
  • 8
    • 84864103186 scopus 로고    scopus 로고
    • Highly aggregated antibody therapeutics can enhance the in vitro innate and late-stage t-cell immune responses
    • Joubert MK, et al. Highly Aggregated Antibody Therapeutics Can Enhance the In Vitro Innate and Late-Stage T-Cell Immune Responses. J. Biol. Chem. 287(30) 2011: 25266-25279.
    • (2011) J. Biol. Chem. , vol.287 , Issue.30 , pp. 25266-25279
    • Joubert, M.K.1
  • 9
    • 84898642873 scopus 로고    scopus 로고
    • Aggregation of human recombinant monoclonal antibodies influences the capacity of dendritic cells to stimulate adaptive t-cell responses in vitro
    • Rombach-Riegraf V, et al. Aggregation of Human Recombinant Monoclonal Antibodies Influences the Capacity of Dendritic Cells to Stimulate Adaptive T-Cell Responses In Vitro. PLoS One 9(1) 2014: e86322.
    • (2014) PLoS One , vol.9 , Issue.1 , pp. e86322
    • Rombach-Riegraf, V.1
  • 10
    • 79851486818 scopus 로고    scopus 로고
    • Interactions and phase behavior of a monoclonal antibody
    • Lewus RA, et al. Interactions and Phase Behavior of a Monoclonal Antibody. Biotechnol. Progr. 27(1) 2011: 280-289.
    • (2011) Biotechnol. Progr. , vol.27 , Issue.1 , pp. 280-289
    • Lewus, R.A.1
  • 11
    • 84923293149 scopus 로고    scopus 로고
    • A Comparative Study of Monoclonal Antibodies. 1: Phase Behavior and Protein-Protein Interactions
    • Lewus RA, et al. A Comparative Study of Monoclonal Antibodies. 1: Phase Behavior and Protein-Protein Interactions. Biotechnol. Progr. 31(1) 2015: 268-276.
    • (2015) Biotechnol. Progr. , vol.31 , Issue.1 , pp. 268-276
    • Lewus, R.A.1
  • 12
    • 27644477360 scopus 로고    scopus 로고
    • Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution
    • Liu J, et al. Reversible Self-Association Increases the Viscosity of a Concentrated Monoclonal Antibody in Aqueous Solution. J. Pharm. Sci. 94(9) 2005: 1928-1940.
    • (2005) J. Pharm. Sci. , vol.94 , Issue.9 , pp. 1928-1940
    • Liu, J.1
  • 13
    • 80053232304 scopus 로고    scopus 로고
    • Opalescence of an igg2 monoclonal antibody solution as it relates to liquid-liquid phase separation
    • Mason BD, et al. Opalescence of an IgG2 Monoclonal Antibody Solution As It Relates to Liquid-Liquid Phase Separation. J. Pharm. Sci. 100(11) 2011: 4587-4596.
    • (2011) J. Pharm. Sci. , vol.100 , Issue.11 , pp. 4587-4596
    • Mason, B.D.1
  • 14
    • 73949139940 scopus 로고    scopus 로고
    • Understanding and modulating opalescence and viscosity in a monoclonal antibody formulation
    • Salinas BA, et al. Understanding and Modulating Opalescence and Viscosity in a Monoclonal Antibody Formulation. J. Pharm. Sci. 99(1) 2010: 82-93.
    • (2010) J. Pharm. Sci. , vol.99 , Issue.1 , pp. 82-93
    • Salinas, B.A.1
  • 15
    • 80053382151 scopus 로고    scopus 로고
    • High-throughput analysis of concentration-dependent antibody self-association
    • Sule SV, et al. High-Throughput Analysis of Concentration-Dependent Antibody Self-Association. Biophys. J. 101(7) 2011: 1749-1757.
    • (2011) Biophys. J. , vol.101 , Issue.7 , pp. 1749-1757
    • Sule, S.V.1
  • 16
    • 79961027385 scopus 로고    scopus 로고
    • Crystallization and liquid-liquid phase separation of monoclonal antibodies and fc-fusion proteins: Screening results
    • Trilisky E, et al. Crystallization and Liquid-Liquid Phase Separation of Monoclonal Antibodies and Fc-Fusion Proteins: Screening Results. Biotechnol. Progr. 27(4) 2011: 1054-1067.
    • (2011) Biotechnol. Progr. , vol.27 , Issue.4 , pp. 1054-1067
    • Trilisky, E.1
  • 17
    • 84899858498 scopus 로고    scopus 로고
    • Quantitative evaluation of colloidal stability of antibody solutions using peg-induced liquid-liquid phase separation
    • Wang Y, et al. Quantitative Evaluation of Colloidal Stability of Antibody Solutions Using PEG-Induced Liquid-Liquid Phase Separation. Mol. Pharm. 11(5) 2014: 1391-1402.
    • (2014) Mol. Pharm. , vol.11 , Issue.5 , pp. 1391-1402
    • Wang, Y.1
  • 18
    • 80053630809 scopus 로고    scopus 로고
    • Phase separation in solutions of monoclonal antibodies and the effect of human serum albumin
    • Wang Y, et al. Phase Separation in Solutions of Monoclonal Antibodies and the Effect of Human Serum Albumin. Proc. Natl. Acad. Sci. USA 108(40) 2010: 16606-16611.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.108 , Issue.40 , pp. 16606-16611
    • Wang, Y.1
  • 19
    • 33846140780 scopus 로고    scopus 로고
    • Antibody structure, instability, and formulation
    • Wang W, et al. Antibody Structure, Instability, and Formulation. J. Pharm. Sci. 96(1) 2007: 1-26.
    • (2007) J. Pharm. Sci. , vol.96 , Issue.1 , pp. 1-26
    • Wang, W.1
  • 20
    • 33845923234 scopus 로고    scopus 로고
    • High throughput screening of protein formulation stability: Practical considerations
    • Capelle MA, Gurny R, Arvinte T. High Throughput Screening of Protein Formulation Stability: Practical Considerations. Eur. J. Pharm. Biopharm. 65(2) 2007: 131-148.
    • (2007) Eur. J. Pharm. Biopharm. , vol.65 , Issue.2 , pp. 131-148
    • Ma, C.1    Gurny, R.2    Arvinte, T.3
  • 21
    • 60649093306 scopus 로고    scopus 로고
    • High throughput methods of assessing protein stability and aggregation
    • Senisterra GA, Finerty PJ Jr. High Throughput Methods of Assessing Protein Stability and Aggregation. Molec. Biosyst. 5(3) 2009: 217-523.
    • (2009) Molec. Biosyst. , vol.5 , Issue.3 , pp. 217-523
    • Senisterra, G.A.1    Finerty, P.J.2
  • 22
    • 77949789023 scopus 로고    scopus 로고
    • High throughput thermostability screening of monoclonal antibody formulations
    • He F, et al. High Throughput Thermostability Screening of Monoclonal Antibody Formulations. J. Pharm. Sci. 99(4) 2010: 1707-1720.
    • (2010) J. Pharm. Sci. , vol.99 , Issue.4 , pp. 1707-1720
    • He, F.1
  • 23
    • 84874115041 scopus 로고
    • Chapter 10: The combined use of the thermofluor assay and thermoq analytical software for the determination of protein stability and buffer optimization as an aid in protein crystallization
    • Ausubel FM, et al., Eds. John Wiley and Sons: Hoboken, NJ
    • Phillips K, de la Pena AH. Chapter 10: The Combined Use of the Thermofluor Assay and ThermoQ Analytical Software for the Determination of Protein Stability and Buffer Optimization As an Aid in Protein Crystallization. Current Protocols in Molecular Biology. Ausubel FM, et al., Eds. John Wiley and Sons: Hoboken, NJ, 1995.
    • (1995) Current Protocols in Molecular Biology
    • Phillips, K.1    De La Pena, A.H.2
  • 24
    • 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 TJ, et al. 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. 100(3) 2011: 1009-1021.
    • (2011) J. Pharm. Sci. , vol.100 , Issue.3 , pp. 1009-1021
    • Gibson, T.J.1
  • 25
    • 84859910800 scopus 로고    scopus 로고
    • Toward a molecular understanding of protein solubility: Increased negative surface charge correlates with increased solubility
    • Kramer RM, et al. Toward a Molecular Understanding of Protein Solubility: Increased Negative Surface Charge Correlates with Increased Solubility. Biophys. J. 102(8) 2012: 1907-1915.
    • (2012) Biophys. J. , vol.102 , Issue.8 , pp. 1907-1915
    • Kramer, R.M.1
  • 26
    • 55749096388 scopus 로고    scopus 로고
    • Measuring and increasing protein solubility
    • Trevino SR, Scholtz JM, Pace CN. Measuring and Increasing Protein Solubility. J. Pharm. Sci. 97(10) 2008: 4155-4166.
    • (2008) J. Pharm. Sci. , vol.97 , Issue.10 , pp. 4155-4166
    • Trevino, S.R.1    Scholtz, J.M.2    Pace, C.N.3
  • 27
    • 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 DD, et al. Native-State Solubility and Transfer Free Energy As Predictive Tools for Selecting Excipients to Include in Protein Formulation Development Studies. J. Pharm. Sci. 101(8) 2012: 2720-2732.
    • (2012) J. Pharm. Sci. , vol.101 , Issue.8 , pp. 2720-2732
    • Banks, D.D.1
  • 28
    • 52449122537 scopus 로고    scopus 로고
    • Self-buffering antibody formulations
    • Gokarn YR, et al. Self-Buffering Antibody Formulations. J. Pharm. Sci. 97(8) 2008: 3051-3066.
    • (2008) J. Pharm. Sci. , vol.97 , Issue.8 , pp. 3051-3066
    • Gokarn, Y.R.1
  • 29
    • 18244380348 scopus 로고    scopus 로고
    • High-density miniaturized thermal shift assays as a general strategy for drug discovery
    • Pantoliano MW, et al. High-Density Miniaturized Thermal Shift Assays As a General Strategy for Drug Discovery. J. Biomol. Screen 6(6) 2001: 429-440.
    • (2001) J. Biomol. Screen , vol.6 , Issue.6 , pp. 429-440
    • Pantoliano, M.W.1
  • 30
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • Ericsson UB, et al. Thermofluor-Based High-Throughput Stability Optimization of Proteins for Structural Studies. Analyt. Biochem. 357(2) 2006: 289-298.
    • (2006) Analyt. Biochem. , vol.357 , Issue.2 , pp. 289-298
    • Ericsson, U.B.1
  • 31
    • 0026514355 scopus 로고
    • Spectrofluorimetric assessment of the surface hydrophobicity of proteins
    • Cardamone M, Puri NK. Spectrofluorimetric Assessment of the Surface Hydrophobicity of Proteins. Biochem. J. 282(2) 1992: 589-593.
    • (1992) Biochem. J. , vol.282 , Issue.2 , pp. 589-593
    • Cardamone, M.1    Puri, N.K.2
  • 32
    • 84888205177 scopus 로고    scopus 로고
    • Linking the solution viscosity of an igg2 monoclonal antibody to its structure as a function of ph and temperature
    • Cheng W, et al. Linking the Solution Viscosity of an IgG2 Monoclonal Antibody to Its Structure As a Function of pH and Temperature. J. Pharm. Sci. 102(12) 2013: 4291-4304.
    • (2013) J. Pharm. Sci. , vol.102 , Issue.12 , pp. 4291-4304
    • Cheng, W.1
  • 33
    • 77951589043 scopus 로고    scopus 로고
    • Detection of igg aggregation by a high throughput method based on extrinsic fluorescence
    • He F, et al. Detection of IgG Aggregation By a High Throughput Method Based on Extrinsic Fluorescence. J. Pharm. Sci. 99(6) 2010: 2598-2608.
    • (2010) J. Pharm. Sci. , vol.99 , Issue.6 , pp. 2598-2608
    • He, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.