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Volumn , Issue , 2006, Pages 331-350

Mutational approach to improve physical stability of protein therapeutics susceptible to aggregation: Role of altered conformation in irreversible precipitation

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EID: 84919843324     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-0-387-36063-8_15     Document Type: Chapter
Times cited : (10)

References (48)
  • 1
    • 0042510222 scopus 로고    scopus 로고
    • Epoetins: Differences and their relevance to immunogenicity
    • A. Haselbeck, Epoetins: differences and their relevance to immunogenicity, Curr. Med. Res. Opin. 19(5), 430-432 (2003).
    • (2003) Curr. Med. Res. Opin. , vol.19 , Issue.5 , pp. 430-432
    • Haselbeck, A.1
  • 2
    • 0027729733 scopus 로고
    • The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation
    • J. L. Cleland, M. F. Powell, and S. J. Shire, The development of stable protein formulations: a close look at protein aggregation, deamidation, and oxidation, Crit. Rev. Ther. Drug Carrier. Syst. 10(4), 307-377 (1993).
    • (1993) Crit. Rev. Ther. Drug Carrier. Syst. , vol.10 , Issue.4 , pp. 307-377
    • Cleland, J.L.1    Powell, M.F.2    Shire, S.J.3
  • 3
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • E. Y. Chi, S. Krishnan, T. W. Randolph, and J. F. Carpenter, Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation, Pharm. Res. 20(9), 1325-1336 (2003).
    • (2003) Pharm. Res. , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 4
    • 0036890693 scopus 로고    scopus 로고
    • The stability factor: Importance in formulation development
    • R. Krishnamurthy and M. C. Manning, The stability factor: importance in formulation development, Cur. Pharm. Biotech. 3(4), 361-371 (2002).
    • (2002) Cur. Pharm. Biotech. , vol.3 , Issue.4 , pp. 361-371
    • Krishnamurthy, R.1    Manning, M.C.2
  • 5
    • 0036111474 scopus 로고    scopus 로고
    • Inverse relationship of protein concentration and aggregation
    • M. J. Treuheit, A. A. Kosky, and D. N. Brems, Inverse relationship of protein concentration and aggregation, Pharm. Res. 19(4), 511-516 (2002).
    • (2002) Pharm. Res. , vol.19 , Issue.4 , pp. 511-516
    • Treuheit, M.J.1    Kosky, A.A.2    Brems, D.N.3
  • 6
    • 0043208919 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks-2003
    • G. Walsh, Biopharmaceutical benchmarks-2003, Nat. Biotech. 21(8), 865-870 (2003).
    • (2003) Nat. Biotech. , vol.21 , Issue.8 , pp. 865-870
    • Walsh, G.1
  • 9
    • 0344874146 scopus 로고    scopus 로고
    • Structure-based substitutions for increased solubility of a designed protein
    • L. K. Mosavi and Z. Peng, Structure-based substitutions for increased solubility of a designed protein, Protein Eng. 16(10), 739-745 (2003).
    • (2003) Protein Eng. , vol.16 , Issue.10 , pp. 739-745
    • Mosavi, L.K.1    Peng, Z.2
  • 10
    • 0032934598 scopus 로고    scopus 로고
    • Hydrophobicity engineering of cholera toxin A1 subunit in the strong adjuvant fusion protein CTA1-DD
    • L. Å Gren, M. Norin, N. Lycke, and B. Löwenadler, Hydrophobicity engineering of cholera toxin A1 subunit in the strong adjuvant fusion protein CTA1-DD, Protein Eng. 12(2), 173-178 (1999).
    • (1999) Protein Eng. , vol.12 , Issue.2 , pp. 173-178
    • Å Gren, L.1    Norin, M.2    Lycke, N.3    Löwenadler, B.4
  • 12
    • 0035009229 scopus 로고    scopus 로고
    • The effect of net charge on the solubility, activity, and stability of ribonuclease Sa
    • K. L. Shaw, G. R. Grimsley, G. I. Yakovlev, A. A. Makarov, and C. N. Pace, The effect of net charge on the solubility, activity, and stability of ribonuclease Sa, Protein Sci. 10(6), 1206-1215 (2001).
    • (2001) Protein Sci. , vol.10 , Issue.6 , pp. 1206-1215
    • Shaw, K.L.1    Grimsley, G.R.2    Yakovlev, G.I.3    Makarov, A.A.4    Pace, C.N.5
  • 13
    • 0031732556 scopus 로고    scopus 로고
    • Engineering the isoelectric point of a renal cell carcinoma targeting antibody greatly enhances scFv solubility
    • P. H. Tan, V. Chu, J. E. Stray, D. K. Hamlin, D. Pettit, D. S. Wilbur, R. L. Vessella, and P. S. Stayton, Engineering the isoelectric point of a renal cell carcinoma targeting antibody greatly enhances scFv solubility, Immunotechnology 4(2), 107-114 (1998).
    • (1998) Immunotechnology , vol.4 , Issue.2 , pp. 107-114
    • Tan, P.H.1    Chu, V.2    Stray, J.E.3    Hamlin, D.K.4    Pettit, D.5    Wilbur, D.S.6    Vessella, R.L.7    Stayton, P.S.8
  • 14
    • 0028139089 scopus 로고
    • Positional cloning of the mouse obese gene and its human homologue
    • Y. Zhang, R. Proenca, M. Maffei, M. Barone, L. Leopold, and J. M. Friedman, Positional cloning of the mouse obese gene and its human homologue, Nature 372(6505), 425-432 (1994).
    • (1994) Nature , vol.372 , Issue.6505 , pp. 425-432
    • Zhang, Y.1    Proenca, R.2    Maffei, M.3    Barone, M.4    Leopold, L.5    Friedman, J.M.6
  • 15
    • 0027258762 scopus 로고
    • The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors
    • C. P. Hill, T. D. Osslund, and D. Eisenberg, The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors, Proc. Nat. Acad. Sci. USA 90(11), 5167-5171 (1993).
    • (1993) Proc. Nat. Acad. Sci. USA , vol.90 , Issue.11 , pp. 5167-5171
    • Hill, C.P.1    Osslund, T.D.2    Eisenberg, D.3
  • 18
    • 0030455390 scopus 로고    scopus 로고
    • The leptin haemopoietic cytokine fold is stabilized by an intrachain disulfide bond
    • F. L. Rock, S. W. Altmann, M. Van Heek, R. A. Kastelein, and J. F. Bazan, The leptin haemopoietic cytokine fold is stabilized by an intrachain disulfide bond, Horm. Metab. Res. 28(12), 649-652 (1996).
    • (1996) Horm. Metab. Res. , vol.28 , Issue.12 , pp. 649-652
    • Rock, F.L.1    Altmann, S.W.2    Van Heek, M.3    Kastelein, R.A.4    Bazan, J.F.5
  • 20
    • 0033105703 scopus 로고    scopus 로고
    • PH-dependent secondary conformation of the peptide hormone leptin in different buffer solutions
    • L.-C. Au, S.-Y. Lin, M.-J. Li, and C.-J. Ho, pH-dependent secondary conformation of the peptide hormone leptin in different buffer solutions, Artif. Cells Blood Substit. Immobil. Biotechol. 27(2), 119-134 (1999).
    • (1999) Artif. Cells Blood Substit. Immobil. Biotechol. , vol.27 , Issue.2 , pp. 119-134
    • Au, L.-C.1    Lin, S.-Y.2    Li, M.-J.3    Ho, C.-J.4
  • 21
    • 0242432378 scopus 로고    scopus 로고
    • PH dependence of structural stability of interleukin-2 and granulocyte colony-stimulating factor
    • M. S. Ricci, C. A. Sarkar, E. M. Fallon, D. A. Lauffenburger, and D. N. Brems. pH dependence of structural stability of interleukin-2 and granulocyte colony-stimulating factor, Protein Sci. 12(5), 1030-1038 (2003).
    • (2003) Protein Sci. , vol.12 , Issue.5 , pp. 1030-1038
    • Ricci, M.S.1    Sarkar, C.A.2    Fallon, E.M.3    Lauffenburger, D.A.4    Brems, D.N.5
  • 22
    • 0027199523 scopus 로고
    • Effect of pH and denaturants on the folding and stability of murine interleukin-6
    • L. D. Ward, J. G. Zhang, G. Checkley, B. Preston, and R. J. Simpson, Effect of pH and denaturants on the folding and stability of murine interleukin-6, Protein Sci. 2(8), 1291-1300 (1993).
    • (1993) Protein Sci. , vol.2 , Issue.8 , pp. 1291-1300
    • Ward, L.D.1    Zhang, J.G.2    Checkley, G.3    Preston, B.4    Simpson, R.J.5
  • 23
    • 9944264495 scopus 로고    scopus 로고
    • Common structural stability properties of 4-helical bundle cytokines: Possible physiological and pharmaceutical consequences
    • M. S. Ricci and D. N. Brems, Common structural stability properties of 4-helical bundle cytokines: Possible physiological and pharmaceutical consequences, Curr. Pharm. Design, 10:3901-3911 (2004).
    • (2004) Curr. Pharm. Design , vol.10 , pp. 3901-3911
    • Ricci, M.S.1    Brems, D.N.2
  • 26
    • 84919860073 scopus 로고    scopus 로고
    • Analysis of the solution behavior of protein pharmaceuticals by laser light scattering photometry
    • Washington, DC: American Chemical Society Symposium Series 675
    • G.-M. Wu, D. Hummel, and A. Herman, Analysis of the solution behavior of protein pharmaceuticals by laser light scattering photometry, in Therapeutic Protein and Peptide Formulation and Delivery (Washington, DC: American Chemical Society Symposium Series 675, 1997).
    • Therapeutic Protein and Peptide Formulation and Delivery , pp. 1997
    • Wu, G.-M.1    Hummel, D.2    Herman, A.3
  • 27
    • 0022412192 scopus 로고
    • Hydrophobicity of amino acid residues in globular proteins
    • G. D. Rose, A. R. Geselowitz, G. J. Lesser, R. H. Lee, and M. H. Zehfus, Hydrophobicity of amino acid residues in globular proteins, Science 229(4716), 834-838 (1985).
    • (1985) Science , vol.229 , Issue.4716 , pp. 834-838
    • Rose, G.D.1    Geselowitz, A.R.2    Lesser, G.J.3    Lee, R.H.4    Zehfus, M.H.5
  • 28
    • 0000484499 scopus 로고
    • Hydrophobic parameters pi of amino-acid side chains from the partitioning of N-acetyl-amino acid amides
    • J. L. Fauchère and V. Pliska, Hydrophobic parameters pi of amino-acid side chains from the partitioning of N-acetyl-amino acid amides, Eur. J. Med. Chem. 18, 369-375 (1983).
    • (1983) Eur. J. Med. Chem. , vol.18 , pp. 369-375
    • Fauchère, J.L.1    Pliska, V.2
  • 30
    • 0023025555 scopus 로고
    • Low concentrations of guanidinium chloride expose apolar surfaces and cause differential perturbation in catalytic intermediates of rhodanese
    • P. Horowitz and N. L. Criscimagna, Low concentrations of guanidinium chloride expose apolar surfaces and cause differential perturbation in catalytic intermediates of rhodanese, J. Biol. Chem. 261(33), 15652-15658 (1986).
    • (1986) J. Biol. Chem. , vol.261 , Issue.33 , pp. 15652-15658
    • Horowitz, P.1    Criscimagna, N.L.2
  • 32
    • 0015997959 scopus 로고
    • Aromatic contributions to circular dichroism spectra of proteins
    • E. H. Strickland, Aromatic contributions to circular dichroism spectra of proteins, CRC Crit. Rev. Biochem. 2(1), 113-175 (1974).
    • (1974) CRC Crit. Rev. Biochem. , vol.2 , Issue.1 , pp. 113-175
    • Strickland, E.H.1
  • 33
    • 0027972684 scopus 로고
    • [Lys (B28), Pro (B29)]-Human insulin: A rapidly absorbed analog of human insulin
    • D. C. Howey, R. R. Bowsher, R. L. Brunelle, and J. R. Woodworth, [Lys (B28), Pro (B29)]-Human insulin: a rapidly absorbed analog of human insulin, Diabetes 43(3), 396-402 (1994).
    • (1994) Diabetes , vol.43 , Issue.3 , pp. 396-402
    • Howey, D.C.1    Bowsher, R.R.2    Brunelle, R.L.3    Woodworth, J.R.4
  • 36
    • 0027138673 scopus 로고
    • Cysteine 17 of recombinant human granulocyte-colony stimulating factor is partially solvent-exposed
    • T. Arakawa, S. J. Prestrelski, L. O. Narhi, T. C. Boone, and W. C. Kenney, Cysteine 17 of recombinant human granulocyte-colony stimulating factor is partially solvent-exposed, J. Protein Chem. 12(5), 525-531 (1993).
    • (1993) J. Protein Chem. , vol.12 , Issue.5 , pp. 525-531
    • Arakawa, T.1    Prestrelski, S.J.2    Narhi, L.O.3    Boone, T.C.4    Kenney, W.C.5
  • 37
    • 0035823594 scopus 로고    scopus 로고
    • Reengineering granulocyte colony-stimulating factor for enhanced stability
    • B. Bishop, D. C. Koay, A. C. Sartorelli, and L. Regan, Reengineering granulocyte colony-stimulating factor for enhanced stability, J. Biol. Chem. 276(36), 33465-33470 (2001).
    • (2001) J. Biol. Chem. , vol.276 , Issue.36 , pp. 33465-33470
    • Bishop, B.1    Koay, D.C.2    Sartorelli, A.C.3    Regan, L.4
  • 38
    • 0025887736 scopus 로고
    • Sitedirected mutagenesis to probe protein folding: Evidence that the formation and aggregation of a bovine growth hormone folding intermediate are dissociable processes
    • S. R. Lehrman, J. L. Tuls, H. A. Havel, R. J. Haskell, S. D. Putnam, and C. S. Tomich, Sitedirected mutagenesis to probe protein folding: Evidence that the formation and aggregation of a bovine growth hormone folding intermediate are dissociable processes, Biochem. 30(23), 5777-5784 (1991).
    • (1991) Biochem. , vol.30 , Issue.23 , pp. 5777-5784
    • Lehrman, S.R.1    Tuls, J.L.2    Havel, H.A.3    Haskell, R.J.4    Putnam, S.D.5    Tomich, C.S.6
  • 40
    • 14444277713 scopus 로고    scopus 로고
    • Interleukin-1 receptor (IL-1R) liquid formulation development using differential scanning calorimetry
    • R. L. Remmele Jr, N. S. Nightlinger, S. Srinivasan, and W. R. Gombotz, Interleukin-1 receptor (IL-1R) liquid formulation development using differential scanning calorimetry, Pharm. Res. 15(2), 200-208 (1998).
    • (1998) Pharm. Res. , vol.15 , Issue.2 , pp. 200-208
    • Remmele, R.L.1    Nightlinger, N.S.2    Srinivasan, S.3    Gombotz, W.R.4
  • 43
    • 0024978382 scopus 로고
    • Thermostability of temperaturesensitive folding mutants of the P22 tailspike protein
    • J. M. Sturtevant, M. H. Yu, C. Haase-Pettingell, and J. King, Thermostability of temperaturesensitive folding mutants of the P22 tailspike protein, J. Biol. Chem. 264(18), 10693-10698 (1989).
    • (1989) J. Biol. Chem. , vol.264 , Issue.18 , pp. 10693-10698
    • Sturtevant, J.M.1    Yu, M.H.2    Haase-Pettingell, C.3    King, J.4
  • 44
    • 0026056333 scopus 로고
    • Identification of global suppressors for temperaturesensitive folding mutations of the P22 tailspike protein
    • B. Fane, R. Villafane, A. Mitraki, and J. King, Identification of global suppressors for temperaturesensitive folding mutations of the P22 tailspike protein, J. Biol. Chem. 266(18), 11640-11648 (1991).
    • (1991) J. Biol. Chem. , vol.266 , Issue.18 , pp. 11640-11648
    • Fane, B.1    Villafane, R.2    Mitraki, A.3    King, J.4
  • 45
    • 0027370268 scopus 로고
    • Mechanism of phage P22 tailspike protein folding mutations
    • M. Danner and R. Seckler, Mechanism of phage P22 tailspike protein folding mutations, Protein Sci. 2(11), 1869-1881 (1993).
    • (1993) Protein Sci. , vol.2 , Issue.11 , pp. 1869-1881
    • Danner, M.1    Seckler, R.2
  • 46
    • 0031582080 scopus 로고    scopus 로고
    • Prevalence of temperature sensitive folding mutations in the parallel beta coil domain of the phage P22 tailspike endorhamnosidase
    • C. Haase-Pettingell and J. King, Prevalence of temperature sensitive folding mutations in the parallel beta coil domain of the phage P22 tailspike endorhamnosidase, J. Mol. Biol. 267(1), 88-102 (1997).
    • (1997) J. Mol. Biol. , vol.267 , Issue.1 , pp. 88-102
    • Haase-Pettingell, C.1    King, J.2
  • 47
    • 0027261309 scopus 로고
    • Inclusion body formation and protein stability in sequence variants of interleukin-1β
    • B. A. Chrunyk, J. Evans, J. Lillquist, P. Young, and R. Wetzel, Inclusion body formation and protein stability in sequence variants of interleukin-1β, J. Biol. Chem. 268(24), 18053-18061 (1993).
    • (1993) J. Biol. Chem. , vol.268 , Issue.24 , pp. 18053-18061
    • Chrunyk, B.A.1    Evans, J.2    Lillquist, J.3    Young, P.4    Wetzel, R.5
  • 48
    • 14744272873 scopus 로고
    • Mutations in human interferon-gamma affecting inclusion body formation identified by a general immunochemical screen
    • R. Wetzel, L. J. Perry, and C. Veilleux, Mutations in human interferon-gamma affecting inclusion body formation identified by a general immunochemical screen, Bio/Tech. 9(8), 731-737 (1991).
    • (1991) Bio/Tech. , vol.9 , Issue.8 , pp. 731-737
    • Wetzel, R.1    Perry, L.J.2    Veilleux, C.3


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