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Volumn 102, Issue 8, 2013, Pages 2424-2439

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

Author keywords

Ammonium sulfate; Antibody; Biologics; Formulation; High throughput technologies; Kosmotrope; Protein aggregation; Protein therapeutic; Solubility; Stability

Indexed keywords

AMMONIUM SULFATE; FC RECEPTOR; HYBRID PROTEIN; MONOCLONAL ANTIBODY; PEGDINETANIB;

EID: 84881026589     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23618     Document Type: Article
Times cited : (26)

References (43)
  • 1
    • 79955666020 scopus 로고    scopus 로고
    • Introduction to current and future protein therapeutics: A protein engineering perspective
    • Carter PJ. 2011. Introduction to current and future protein therapeutics: A protein engineering perspective. Exp Cell Res 317:1261-1269.
    • (2011) Exp Cell Res , vol.317 , pp. 1261-1269
    • Carter, P.J.1
  • 2
    • 77950666079 scopus 로고    scopus 로고
    • Fresh from the biologic pipeline-2009
    • Sheridan C. 2010. Fresh from the biologic pipeline-2009. Nat Biotechnol 28:307-310.
    • (2010) Nat Biotechnol , vol.28 , pp. 307-310
    • Sheridan, C.1
  • 3
    • 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
  • 4
    • 79956103081 scopus 로고    scopus 로고
    • Aggregates in monoclonal antibody manufacturing processes
    • Vázquez-Rey M, Lang DA. 2011. Aggregates in monoclonal antibody manufacturing processes. Biotechnol Bioeng 108:1494-1508.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 1494-1508
    • Vázquez-Rey, M.1    Lang, D.A.2
  • 5
    • 79851475357 scopus 로고    scopus 로고
    • Immunogenicity of protein therapeutics: The key causes, consequences and challenges
    • Baker MP, Reynolds HM, Lumicisi B, Bryson CJ. 2010. Immunogenicity of protein therapeutics: The key causes, consequences and challenges. Self Nonself 1:314-322.
    • (2010) Self Nonself , vol.1 , pp. 314-322
    • Baker, M.P.1    Reynolds, H.M.2    Lumicisi, B.3    Bryson, C.J.4
  • 6
    • 59349083966 scopus 로고    scopus 로고
    • Protein aggregation kinetics, mechanism, and curve- fitting: A review of the literature
    • Morris AM, Watzky MA, Finke RG. 2009. Protein aggregation kinetics, mechanism, and curve- fitting: A review of the literature. Biochim Biophys Acta 1794:375-397.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 375-397
    • Morris, A.M.1    Watzky, M.A.2    Finke, R.G.3
  • 7
    • 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 286:25118-25133.
    • (2011) J Biol Chem , vol.286 , pp. 25118-25133
    • Joubert, M.K.1    Luo, Q.2    Nashed-Samuel, Y.3    Wypych, J.4    Narhi, L.O.5
  • 8
    • 67449132077 scopus 로고    scopus 로고
    • Principles, approaches, and challenges for predicting protein aggregation rates and shelf life
    • Weiss WF, Young TM, Roberts CJ. 2009. Principles, approaches, and challenges for predicting protein aggregation rates and shelf life. J Pharm Sci 98:1246-1277.
    • (2009) J Pharm Sci , vol.98 , pp. 1246-1277
    • Weiss, W.F.1    Young, T.M.2    Roberts, C.J.3
  • 9
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • Roberts CJ. 2007. Non-native protein aggregation kinetics. Biotechnol Bioeng 98:927-938.
    • (2007) Biotechnol Bioeng , vol.98 , pp. 927-938
    • Roberts, C.J.1
  • 10
    • 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 38:79-87.
    • (2009) Eur J Pharm Sci , vol.38 , pp. 79-87
    • Hawe, A.1    Kasper, J.C.2    Friess, W.3    Jiskoot, W.4
  • 11
    • 68949085124 scopus 로고    scopus 로고
    • Protein aggregation: Pathways, induction factors and analysis
    • Mahler HC, Friess W, Grauschopf U, Kiese S. 2009. Protein aggregation: Pathways, induction factors and analysis. J Pharm Sci 98:2909-2934.
    • (2009) J Pharm Sci , vol.98 , pp. 2909-2934
    • Mahler, H.C.1    Friess, W.2    Grauschopf, U.3    Kiese, S.4
  • 12
  • 13
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang, W. 2005. Protein aggregation and its inhibition in biopharmaceutics. Int J Pharm 289:1-30.
    • (2005) Int J Pharm , vol.289 , pp. 1-30
    • Wang, W.1
  • 15
    • 80054717076 scopus 로고    scopus 로고
    • Protein-excipient interactions: Mechanisms and biophysical characterization applied to protein formulation development
    • Kamerzell TJ, Esfandiary R, Joshi SB, Middaugh CR, Volkin DB. 2011. Protein-excipient interactions: Mechanisms and biophysical characterization applied to protein formulation development. Adv Drug Deliv Rev 63:1118-1159.
    • (2011) Adv Drug Deliv Rev , vol.63 , pp. 1118-1159
    • Kamerzell, T.J.1    Esfandiary, R.2    Joshi, S.B.3    Middaugh, C.R.4    Volkin, D.B.5
  • 18
    • 84855575327 scopus 로고    scopus 로고
    • A screening tool for therapeutic monoclonal antibodies: Identifying the most stable protein and its best formulation based on thioflavin T binding
    • Kayser V, Chennamsetty N, Voynov V, Helk B, Forrer K, Trout BL. 2012. A screening tool for therapeutic monoclonal antibodies: Identifying the most stable protein and its best formulation based on thioflavin T binding. Biotechnol J. 7:127-132.
    • (2012) Biotechnol J. , vol.7 , pp. 127-132
    • Kayser, V.1    Chennamsetty, N.2    Voynov, V.3    Helk, B.4    Forrer, K.5    Trout, B.L.6
  • 19
    • 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 99:1707-1720.
    • (2010) J Pharm Sci , vol.99 , pp. 1707-1720
    • He, F.1    Hogan, S.2    Latypov, R.F.3    Narhi, L.O.4    Razinkov, V.I.5
  • 20
    • 33748525884 scopus 로고    scopus 로고
    • Computational models for the prediction of polypeptide aggregation propensity
    • Caflisch A. 2006. Computational models for the prediction of polypeptide aggregation propensity. Curr Opin Chem Biol 10:437-444.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 437-444
    • Caflisch, A.1
  • 21
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla AM, Rousseau F, Schymkowitz J, Serrano L. 2004. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat Biotechnol 22:1302-1306.
    • (2004) Nat Biotechnol , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 23
    • 0000116343 scopus 로고
    • Studies in the physical chemistry of the proteins. VIII. The solubility of hemoglobin in concentrated salt solutions. A study of the salting-out of proteins
    • Green AA. 1931. Studies in the physical chemistry of the proteins. VIII. The solubility of hemoglobin in concentrated salt solutions. A study of the salting-out of proteins. J Biol Chem 93:495-516.
    • (1931) J Biol Chem , vol.93 , pp. 495-516
    • Green, A.A.1
  • 24
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin RL. 1996. How Hofmeister ion interactions affect protein stability. Biophys J 71:2056-2063.
    • (1996) Biophys J , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 25
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • Young L, Jernigan RL, Covell DG. 1994. A role for surface hydrophobicity in protein-protein recognition. Protein Sci 3:717-729.
    • (1994) Protein Sci , vol.3 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3
  • 26
    • 44349092523 scopus 로고    scopus 로고
    • Hydrophobic clusters in protein structures
    • Arunachalam J, Gautham N. 2008. Hydrophobic clusters in protein structures. Proteins 71:2012-2025.
    • (2008) Proteins , vol.71 , pp. 2012-2025
    • Arunachalam, J.1    Gautham, N.2
  • 27
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink, AL. 1998. Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Fold Des 3:R9-R23.
    • (1998) Fold Des , vol.3
    • Fink, A.L.1
  • 28
    • 55749096388 scopus 로고    scopus 로고
    • Measuring and increasing protein solubility
    • Trevino SR, Scholtz JM, Pace CN. 2008. Measuring and increasing protein solubility. J Pharm Sci 97:4155-4166.
    • (2008) J Pharm Sci , vol.97 , pp. 4155-4166
    • Trevino, S.R.1    Scholtz, J.M.2    Pace, C.N.3
  • 29
    • 33846374339 scopus 로고    scopus 로고
    • Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa
    • Trevino SR, Scholtz JM, Pace CN. 2007. Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa. J Mol Biol 366:449-460.
    • (2007) J Mol Biol , vol.366 , pp. 449-460
    • Trevino, S.R.1    Scholtz, J.M.2    Pace, C.N.3
  • 32
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger P, Hudson PJ. 2005. Engineered antibody fragments and the rise of single domains. Nat Biotechnol 23:1126-1136.
    • (2005) Nat Biotechnol , vol.23 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 34
    • 11944271430 scopus 로고
    • Solubility as a function of protein structure and solvent components
    • Schein CH. 1990. Solubility as a function of protein structure and solvent components. Biotechnology 8:308-317.
    • (1990) Biotechnology , vol.8 , pp. 308-317
    • Schein, C.H.1
  • 35
    • 84859910800 scopus 로고    scopus 로고
    • Toward a molecular understanding of protein solubility: Increased negative surface charge correlates with increased solubility
    • Kramer RM, Shende VR, Motl N, Pace CN, Scholtz JM. 2012. Toward a molecular understanding of protein solubility: Increased negative surface charge correlates with increased solubility. Biophys J 102:1907-1915.
    • (2012) Biophys J , vol.102 , pp. 1907-1915
    • Kramer, R.M.1    Shende, V.R.2    Motl, N.3    Pace, C.N.4    Scholtz, J.M.5
  • 36
    • 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, Mccarty K, Mcfadyen IJ, Cash E, Dalmonte P, Hinds KD, Dinerman AA, Alvarez JC, Volkin DB. 2011. 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 100:1009-1021.
    • (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
  • 37
    • 0029584509 scopus 로고
    • Estimation of recombinant bovine somatotropin solubility by excluded-volume interaction with polyethylene glycols
    • Stevenson CL, Hageman MJ. 1995. Estimation of recombinant bovine somatotropin solubility by excluded-volume interaction with polyethylene glycols. Pharm Res. 12:1671-1676.
    • (1995) Pharm Res. , vol.12 , pp. 1671-1676
    • Stevenson, C.L.1    Hageman, M.J.2
  • 38
    • 84867065769 scopus 로고    scopus 로고
    • Fc-fusion proteins: New developments and future perspectives
    • Czajkowsky DM, Hu J, Shao Z, Pleass RJ. 2012. Fc-fusion proteins: New developments and future perspectives. EMBO Mol Med 4:1015-1028.
    • (2012) EMBO Mol Med , vol.4 , pp. 1015-1028
    • Czajkowsky, D.M.1    Hu, J.2    Shao, Z.3    Pleass, R.J.4
  • 41
    • 0022147096 scopus 로고
    • The Hofmeister effect and the behaviour of water at interfaces
    • Collins KD, Washabaugh MW. 1985. The Hofmeister effect and the behaviour of water at interfaces. Q Rev Biophys 18:323-422.
    • (1985) Q Rev Biophys , vol.18 , pp. 323-422
    • Collins, K.D.1    Washabaugh, M.W.2
  • 42
    • 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, Latypov RF, Ketchem RR, Woodard J, Scavezze JL, Siska CC, Razinkov VI. 2012. Native-state solubility and transfer free energy as predictive tools for selecting excipients to include in protein formulation development studies. J Pharm Sci 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


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