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Volumn 72, Issue , 2013, Pages 59-64

Analysis and characterization of aggregation of a therapeutic Fc-fusion protein

Author keywords

Fc fusion protein; Free thiols; Partially frozen; Protein aggregation; Protein stability

Indexed keywords

FC FUSION PROTEIN; HYBRID PROTEIN; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84869053296     PISSN: 07317085     EISSN: 1873264X     Source Type: Journal    
DOI: 10.1016/j.jpba.2012.09.010     Document Type: Article
Times cited : (11)

References (35)
  • 1
    • 0031241608 scopus 로고    scopus 로고
    • Degradative covalent reactions important to protein stability
    • Volkin D.B., March H., Middaugh C.R. Degradative covalent reactions important to protein stability. Mol. Biotechnol. 1997, 8:105-122.
    • (1997) Mol. Biotechnol. , vol.8 , pp. 105-122
    • Volkin, D.B.1    March, H.2    Middaugh, C.R.3
  • 3
    • 0032782071 scopus 로고    scopus 로고
    • Instability stabilization, and formulation of liquid protein pharmaceuticals
    • Wang W. Instability stabilization, and formulation of liquid protein pharmaceuticals. Int. J. Pharm. 1999, 185:129-188.
    • (1999) Int. J. Pharm. , vol.185 , pp. 129-188
    • Wang, W.1
  • 4
    • 33748041958 scopus 로고    scopus 로고
    • Effect of protein aggregates: an immunological perspective
    • Rosenberg A.S. Effect of protein aggregates: an immunological perspective. AAPS J. 2006, 8:E501-E507.
    • (2006) AAPS J. , vol.8
    • Rosenberg, A.S.1
  • 5
    • 68949135230 scopus 로고    scopus 로고
    • Immunogenicity of aggregates of recombinant human growth hormone in mouse models
    • Fradkin A.H., Carpenter J.F., Randolph T.W. Immunogenicity of aggregates of recombinant human growth hormone in mouse models. J. Pharm. Sci. 2009, 98:3247-3264.
    • (2009) J. Pharm. Sci. , vol.98 , pp. 3247-3264
    • Fradkin, A.H.1    Carpenter, J.F.2    Randolph, T.W.3
  • 6
    • 3042761213 scopus 로고    scopus 로고
    • Structure-immunogenicity relationships of therapeutic proteins
    • Hermeling S., Crommelin D., Schellekens H., Jiskoot W. Structure-immunogenicity relationships of therapeutic proteins. Pharm. Res. 2004, 21:897-903.
    • (2004) Pharm. Res. , vol.21 , pp. 897-903
    • Hermeling, S.1    Crommelin, D.2    Schellekens, H.3    Jiskoot, W.4
  • 7
    • 77956355090 scopus 로고    scopus 로고
    • Increased aggregation propensity of IgG2 subclass over IgG1: role of conformational changes and covalent character in isolated aggregates
    • Franey H., Brych S.R., Kolvenbach C.G., Rajan R.S. Increased aggregation propensity of IgG2 subclass over IgG1: role of conformational changes and covalent character in isolated aggregates. Protein Sci. 2010, 19:1601-1615.
    • (2010) Protein Sci. , vol.19 , pp. 1601-1615
    • Franey, H.1    Brych, S.R.2    Kolvenbach, C.G.3    Rajan, R.S.4
  • 8
    • 0029114196 scopus 로고
    • Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments
    • Schweers O., Mandelkow E.M., Biernat J., Mandelkow E. Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:8463-8467.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8463-8467
    • Schweers, O.1    Mandelkow, E.M.2    Biernat, J.3    Mandelkow, E.4
  • 9
    • 74049123779 scopus 로고    scopus 로고
    • Characterization of antibody aggregation: role of buried unpaired cysteines in particle formation
    • Brych S.R., Gokarn Y.R., Hultgen H., Stevenson R.J., Rajan R., Matsumura M. Characterization of antibody aggregation: role of buried unpaired cysteines in particle formation. J. Pharm. Sci. 2010, 99:764-781.
    • (2010) J. Pharm. Sci. , vol.99 , pp. 764-781
    • Brych, S.R.1    Gokarn, Y.R.2    Hultgen, H.3    Stevenson, R.J.4    Rajan, R.5    Matsumura, M.6
  • 10
    • 39749120684 scopus 로고    scopus 로고
    • Removal of cysteinylation from an unpaired sulfhydryl in the variable region of a recombinant monoclonal IgG1 antibody improves homogeneity stability, and biological activity
    • Banks D.D., Gadgil H.S., Pipes G.D., Bondarenko P.V., Hobbs V., Scavezze J.L., Kim J., Jiang X.-R., Mukku V., Dillon T.M. Removal of cysteinylation from an unpaired sulfhydryl in the variable region of a recombinant monoclonal IgG1 antibody improves homogeneity stability, and biological activity. J. Pharm. Sci. 2008, 97:764-779.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 764-779
    • Banks, D.D.1    Gadgil, H.S.2    Pipes, G.D.3    Bondarenko, P.V.4    Hobbs, V.5    Scavezze, J.L.6    Kim, J.7    Jiang, X.-R.8    Mukku, V.9    Dillon, T.M.10
  • 11
    • 33746273552 scopus 로고    scopus 로고
    • Identification of cysteinylation of a free cysteine in the Fab region of a recombinant monoclonal IgG1 antibody using Lys-C limited proteolysis coupled with LC/MS analysis
    • Gadgil H.S., Bondarenko P.V., Pipes G.D., Dillon T.M., Banks D., Abel J., Kleemann G.R., Treuheit M.J. Identification of cysteinylation of a free cysteine in the Fab region of a recombinant monoclonal IgG1 antibody using Lys-C limited proteolysis coupled with LC/MS analysis. Anal. Biochem. 2006, 355:165-174.
    • (2006) Anal. Biochem. , vol.355 , pp. 165-174
    • Gadgil, H.S.1    Bondarenko, P.V.2    Pipes, G.D.3    Dillon, T.M.4    Banks, D.5    Abel, J.6    Kleemann, G.R.7    Treuheit, M.J.8
  • 13
    • 68949085124 scopus 로고    scopus 로고
    • Protein aggregation: pathways, induction factors and analysis
    • Mahler H.-C., Friess W., Grauschopf U., Kiese S. Protein aggregation: pathways, induction factors and analysis. J. Pharm. Sci. 2009, 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
  • 14
    • 79960128166 scopus 로고    scopus 로고
    • Classification and characterization of therapeutic antibody aggregates
    • Joubert M.K., Luo Q., Nashed-Samuel Y., Wypych J., Narhi L.O. Classification and characterization of therapeutic antibody aggregates. J. Biol. Chem. 2011, 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
  • 15
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang W. Protein aggregation and its inhibition in biopharmaceutics. Int. J. Pharm. 2005, 289:1-30.
    • (2005) Int. J. Pharm. , vol.289 , pp. 1-30
    • Wang, W.1
  • 16
    • 7644230941 scopus 로고    scopus 로고
    • De novo peptide sequencing based on a divide-and-conquer algorithm and peptide tandem spectrum simulation
    • Zhang Z. De novo peptide sequencing based on a divide-and-conquer algorithm and peptide tandem spectrum simulation. Anal. Chem. 2004, 76:6374-6383.
    • (2004) Anal. Chem. , vol.76 , pp. 6374-6383
    • Zhang, Z.1
  • 17
    • 0032780618 scopus 로고    scopus 로고
    • Noncomplexing tertiary amines as better buffers covering the range of pH 3-11, temperature dependence of their acid dissociation constant
    • Kandegedara A., Rorabacher D.B. Noncomplexing tertiary amines as better buffers covering the range of pH 3-11, temperature dependence of their acid dissociation constant. Anal. Chem. 1999, 71:3140-3144.
    • (1999) Anal. Chem. , vol.71 , pp. 3140-3144
    • Kandegedara, A.1    Rorabacher, D.B.2
  • 18
    • 33846178245 scopus 로고    scopus 로고
    • Glimpses into the realm of freeze-drying: fundamental issues
    • Informa Healthcare USA, Inc., New York, NY, L. Rey, J.C. May (Eds.)
    • Rey L. Glimpses into the realm of freeze-drying: fundamental issues. Freeze-Drying/Lyophilization of Pharmaceutical and Biological Products 2007, 1-32. Informa Healthcare USA, Inc., New York, NY. L. Rey, J.C. May (Eds.).
    • (2007) Freeze-Drying/Lyophilization of Pharmaceutical and Biological Products , pp. 1-32
    • Rey, L.1
  • 19
    • 0017850021 scopus 로고
    • Oxidation of sulfhydryl groups in lactate dehydrogenase under high hydrostatic pressure
    • Schmid G., Lüdemann H.-D., Jaenicke R. Oxidation of sulfhydryl groups in lactate dehydrogenase under high hydrostatic pressure. Eur. J. Biochem. 1978, 86:219-224.
    • (1978) Eur. J. Biochem. , vol.86 , pp. 219-224
    • Schmid, G.1    Lüdemann, H.-D.2    Jaenicke, R.3
  • 20
    • 33747355902 scopus 로고
    • Reactivity of sulfhydryl and disulfide in proteins. III. Oxidation with ferricyanide of sulfhydryl in native and denatured bovine serum albumin
    • Kolthoff I.M., Anastasi A. Reactivity of sulfhydryl and disulfide in proteins. III. Oxidation with ferricyanide of sulfhydryl in native and denatured bovine serum albumin. J. Am. Chem. Soc. 1958, 80:4248-4250.
    • (1958) J. Am. Chem. Soc. , vol.80 , pp. 4248-4250
    • Kolthoff, I.M.1    Anastasi, A.2
  • 21
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: predominance of native intermediates
    • Weissman J., Kim P. Reexamination of the folding of BPTI: predominance of native intermediates. Science 1991, 253:1386-1393.
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.1    Kim, P.2
  • 22
    • 0031017896 scopus 로고    scopus 로고
    • Refined structure of an intact IgG2a monoclonal antibody
    • Harris L.J., Larson S.B., Hasel K.W., McPherson A. Refined structure of an intact IgG2a monoclonal antibody. Biochemistry 1997, 36:1581-1597.
    • (1997) Biochemistry , vol.36 , pp. 1581-1597
    • Harris, L.J.1    Larson, S.B.2    Hasel, K.W.3    McPherson, A.4
  • 24
    • 0013060318 scopus 로고
    • Chapter 14, storage stabilization of proteins
    • The Humana Press Inc., Totowa, NJ, F. Franks (Ed.)
    • Franks F. Chapter 14, storage stabilization of proteins. Protein Biotechnology, Isolation Characterization and Stability 1993, 489-531. The Humana Press Inc., Totowa, NJ. F. Franks (Ed.).
    • (1993) Protein Biotechnology, Isolation Characterization and Stability , pp. 489-531
    • Franks, F.1
  • 25
    • 0032078241 scopus 로고    scopus 로고
    • Freeze-drying of bioproducts: putting principles into practice
    • Franks F. Freeze-drying of bioproducts: putting principles into practice. Eur. J. Pharm. Biopharm. 1998, 45:221-229.
    • (1998) Eur. J. Pharm. Biopharm. , vol.45 , pp. 221-229
    • Franks, F.1
  • 27
    • 0030770631 scopus 로고    scopus 로고
    • Rational design of stable lyophilized protein formulations: some practical advice
    • Carpenter J.F., Pikal M.J., Chang B.S., Randolph T.W. Rational design of stable lyophilized protein formulations: some practical advice. Pharm. Res. 1997, 14:969-975.
    • (1997) Pharm. Res. , vol.14 , pp. 969-975
    • Carpenter, J.F.1    Pikal, M.J.2    Chang, B.S.3    Randolph, T.W.4
  • 28
    • 0016204251 scopus 로고
    • Phase diagram relationships in cryobiology
    • Cocks F.H., Brower W.E. Phase diagram relationships in cryobiology. Cryobiology 1974, 11:340-358.
    • (1974) Cryobiology , vol.11 , pp. 340-358
    • Cocks, F.H.1    Brower, W.E.2
  • 29
    • 33644983601 scopus 로고    scopus 로고
    • Physical characterization of pharmaceutical formulations in frozen and freeze-dried solid states: techniques and applications in freeze-drying development
    • Liu J. Physical characterization of pharmaceutical formulations in frozen and freeze-dried solid states: techniques and applications in freeze-drying development. Pharm. Dev. Technol. 2006, 11:3-28.
    • (2006) Pharm. Dev. Technol. , vol.11 , pp. 3-28
    • Liu, J.1
  • 30
    • 0025142518 scopus 로고
    • Glass-rubber transitions of cellulosic polymers by dynamic mechanical analysis
    • Kararli T.T., Hurlbut J.B., Needham T.E. Glass-rubber transitions of cellulosic polymers by dynamic mechanical analysis. J. Pharm. Sci. 1990, 79:845-848.
    • (1990) J. Pharm. Sci. , vol.79 , pp. 845-848
    • Kararli, T.T.1    Hurlbut, J.B.2    Needham, T.E.3
  • 31
    • 0029056710 scopus 로고
    • Dielectric analysis in the characterization of amorphous pharmaceutical solids. 1. Molecular mobility in poly(vinylpyrrolidone)-water systems in the glassy state
    • Duddu S.P., Sokoloski T.D. Dielectric analysis in the characterization of amorphous pharmaceutical solids. 1. Molecular mobility in poly(vinylpyrrolidone)-water systems in the glassy state. J. Pharm. Sci. 1995, 84:773-776.
    • (1995) J. Pharm. Sci. , vol.84 , pp. 773-776
    • Duddu, S.P.1    Sokoloski, T.D.2
  • 32
    • 0003318044 scopus 로고
    • Separation by precipitation
    • Springer Science+Business Media, LLC., New York, NY, R.K. Scopes (Ed.)
    • Scopes R.K. Separation by precipitation. Protein Purification: Principles and Practice 1994, 71-84. Springer Science+Business Media, LLC., New York, NY. R.K. Scopes (Ed.).
    • (1994) Protein Purification: Principles and Practice , pp. 71-84
    • Scopes, R.K.1
  • 33
    • 84869063871 scopus 로고    scopus 로고
    • Chapter 2, principles of HIC
    • Amersham Pharmacia Biotech UK Limited, Buckinghamshire, England, S.E. Builder (Ed.)
    • Builder S.E. Chapter 2, principles of HIC. Hydrophobic Interaction Chromatography, Principles and Methods 1999, 11-18. Amersham Pharmacia Biotech UK Limited, Buckinghamshire, England. S.E. Builder (Ed.).
    • (1999) Hydrophobic Interaction Chromatography, Principles and Methods , pp. 11-18
    • Builder, S.E.1
  • 34
    • 0020477047 scopus 로고
    • Preferential interactions of proteins with salts in concentrated solutions
    • Arakawa T., Timasheff S.N. Preferential interactions of proteins with salts in concentrated solutions. Biochemistry 1982, 21:6545-6552.
    • (1982) Biochemistry , vol.21 , pp. 6545-6552
    • Arakawa, T.1    Timasheff, S.N.2
  • 35
    • 0017623134 scopus 로고
    • Salt effect on hydrophobic interactions in precipitation and chromatography of proteins: an interpretation of the lyotropic series
    • Melander W., Horváth C. Salt effect on hydrophobic interactions in precipitation and chromatography of proteins: an interpretation of the lyotropic series. Arch. Biochem. Biophys. 1977, 183:200-215.
    • (1977) Arch. Biochem. Biophys. , vol.183 , pp. 200-215
    • Melander, W.1    Horváth, C.2


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