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Volumn 100, Issue 12, 2011, Pages 5100-5114

Demonstrating the stability of albinterferon alfa-2b in the presence of silicone oil

Author keywords

Analytical biochemistry; Analytical ultracentrifugation; Circular dichroism; Freeze drying lyophilization; FTIR; Protein aggregation; Protein delivery; Protein formulation; Protein structure; Stability

Indexed keywords

ALBINTERFERON ALPHA2B; ALBUMIN; PLACEBO; SILICONE OIL;

EID: 80054886521     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.22704     Document Type: Article
Times cited : (28)

References (37)
  • 1
    • 33947661498 scopus 로고    scopus 로고
    • Immunogenicity of therapeutic proteins. Part 2: Impact of container closures
    • Sharma B. 2007. Immunogenicity of therapeutic proteins. Part 2: Impact of container closures. Biotech Adv 25:318-324.
    • (2007) Biotech Adv , vol.25 , pp. 318-324
    • Sharma, B.1
  • 2
    • 0014267132 scopus 로고
    • Panel discussion: Siliconization of parenteral packaging components. I. Siliconization as applied to containers and closures
    • Riffkin C. 1968. Panel discussion: Siliconization of parenteral packaging components. I. Siliconization as applied to containers and closures. Bull Parenter Drug Assoc 22:66-69.
    • (1968) Bull Parenter Drug Assoc , vol.22 , pp. 66-69
    • Riffkin, C.1
  • 3
    • 0014266490 scopus 로고
    • Panel discussion: Siliconization of parenteral packaging components. II. Siliconization as applied to hypodermic needles
    • Elias W. 1968. Panel discussion: Siliconization of parenteral packaging components. II. Siliconization as applied to hypodermic needles. Bull Parenter Drug Assoc 22: 70-71.
    • (1968) Bull Parenter Drug Assoc , vol.22 , pp. 70-71
    • Elias, W.1
  • 4
    • 0024515587 scopus 로고
    • Silicone oil contamination of insulin
    • Chantelau E. 1989. Silicone oil contamination of insulin. Diabet Med 6:278.
    • (1989) Diabet Med , vol.6 , pp. 278
    • Chantelau, E.1
  • 5
    • 0023441166 scopus 로고
    • Clouding and deactivation of clear (regular) human insulin: Association with silicone oil from disposable syringes
    • Bernstein RK. 1987. Clouding and deactivation of clear (regular) human insulin: Association with silicone oil from disposable syringes? Diabet Care 10:786-790.
    • (1987) Diabet Care , vol.10 , pp. 786-790
    • Bernstein, R.K.1
  • 6
    • 0027729733 scopus 로고
    • The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation
    • Cleland J, Powell M, Shire S. 1993. The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation. Crit Rev Ther Drug Carrier Syst 10:307-377.
    • (1993) Crit Rev Ther Drug Carrier Syst , vol.10 , pp. 307-377
    • Cleland, J.1    Powell, M.2    Shire, S.3
  • 7
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An immunologic perspective
    • Rosenburg A. 2006. Effects of protein aggregates: An immunologic perspective. AAPS J 8:501-507.
    • (2006) AAPS J , vol.8 , pp. 501-507
    • Rosenburg, A.1
  • 8
    • 0032025990 scopus 로고    scopus 로고
    • Protein-silicone interactions: How compatible are the two species
    • Bartzoka V, Brook M, McDermott M. 1998. Protein-silicone interactions: How compatible are the two species? Langmuir 14:1887-1891.
    • (1998) Langmuir , vol.14 , pp. 1887-1891
    • Bartzoka, V.1    Brook, M.2    McDermott, M.3
  • 9
    • 17744363305 scopus 로고    scopus 로고
    • Silicone oil induced aggregation of proteins
    • Jones L, Kaufmann A, Middaugh C. 2005. Silicone oil induced aggregation of proteins. J Pharm Sci 94:918-927.
    • (2005) J Pharm Sci , vol.94 , pp. 918-927
    • Jones, L.1    Kaufmann, A.2    Middaugh, C.3
  • 10
    • 33847683955 scopus 로고    scopus 로고
    • Quantitation of aggregate levels in a recombinant humanized monoclonal antibody formulation by size-exclusion chromatography, asymmetrical flow field fractionation, and sedimentation velocity
    • Gabrielson J, Brader M, Pekar A, Mathis K, Winter G, Carpenter J, Randolph T. 2007. Quantitation of aggregate levels in a recombinant humanized monoclonal antibody formulation by size-exclusion chromatography, asymmetrical flow field fractionation, and sedimentation velocity. J Pharm Sci 96:268-279.
    • (2007) J Pharm Sci , vol.96 , pp. 268-279
    • Gabrielson, J.1    Brader, M.2    Pekar, A.3    Mathis, K.4    Winter, G.5    Carpenter, J.6    Randolph, T.7
  • 11
    • 68949136656 scopus 로고    scopus 로고
    • Silicone-oil and agitation-induced aggregation of a monoclonal antibody in aqueous solution
    • Thirumangalathu R, Krishnan S, Ricci M, Brems D, Randolph T, Carpenter J. 2009. Silicone-oil and agitation-induced aggregation of a monoclonal antibody in aqueous solution. J Pharm Sci 98:3167-3181.
    • (2009) J Pharm Sci , vol.98 , pp. 3167-3181
    • Thirumangalathu, R.1    Krishnan, S.2    Ricci, M.3    Brems, D.4    Randolph, T.5    Carpenter, J.6
  • 14
    • 77951552352 scopus 로고    scopus 로고
    • Quantification and characterization of subvisible proteinaceous particles in opalescent mAB formulations using micro-flow imaging
    • Sharma D, Oma P, Pollo M, Sukumar M. 2010. Quantification and characterization of subvisible proteinaceous particles in opalescent mAB formulations using micro-flow imaging. J Pharm Sci 99:2628-2642.
    • (2010) J Pharm Sci , vol.99 , pp. 2628-2642
    • Sharma, D.1    Oma, P.2    Pollo, M.3    Sukumar, M.4
  • 15
    • 78650577461 scopus 로고    scopus 로고
    • Subvisible particle counting provides a sensitive method of detecting and quantifying aggregation of monoclonal antibody caused by freeze-thawing: insights into the roles of particles in the protein aggregation pathway
    • Barnard J, Singh S, Randolph T, Carpenter J. 2011. Subvisible particle counting provides a sensitive method of detecting and quantifying aggregation of monoclonal antibody caused by freeze-thawing: insights into the roles of particles in the protein aggregation pathway. J Pharm Sci 100(2):492-503.
    • (2011) J Pharm Sci , vol.100 , Issue.2 , pp. 492-503
    • Barnard, J.1    Singh, S.2    Randolph, T.3    Carpenter, J.4
  • 16
    • 85030495719 scopus 로고    scopus 로고
    • ICH Q6B test procedures and acceptance criteria for biotechnological/biological products-8/18/1999.
    • ICH Q6B test procedures and acceptance criteria for biotechnological/biological products-8/18/1999.
  • 17
    • 79952222483 scopus 로고    scopus 로고
    • Direct visualization of protein adsorption to primary containers by gold nanoparticles
    • Eu B, Cairns A, Ding G, Cao X, Wen Z. 2011. Direct visualization of protein adsorption to primary containers by gold nanoparticles. J Pharm Sci 100:1663-1670.
    • (2011) J Pharm Sci , vol.100 , pp. 1663-1670
    • Eu, B.1    Cairns, A.2    Ding, G.3    Cao, X.4    Wen, Z.5
  • 18
    • 21344469442 scopus 로고    scopus 로고
    • Effects of Tween 20® and Tween 80® on the stability of albutropin during agitation
    • Chou D, Krishnamurthy R, Randolph T, Carpenter J, Manning M. 2005. Effects of Tween 20® and Tween 80® on the stability of albutropin during agitation. J Pharm Sci 94:1368-1381.
    • (2005) J Pharm Sci , vol.94 , pp. 1368-1381
    • Chou, D.1    Krishnamurthy, R.2    Randolph, T.3    Carpenter, J.4    Manning, M.5
  • 19
    • 0031688168 scopus 로고    scopus 로고
    • Sedimentation analysis of non-interacting and self-associating solutes using numerical solutions to the Lamm equation modeling
    • Schuck P. 1998. Sedimentation analysis of non-interacting and self-associating solutes using numerical solutions to the Lamm equation modeling. Biophys J 75:1503-1512.
    • (1998) Biophys J , vol.75 , pp. 1503-1512
    • Schuck, P.1
  • 20
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck P. 2000. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys J 78:1606-1621.
    • (2000) Biophys J , vol.78 , pp. 1606-1621
    • Schuck, P.1
  • 21
    • 0034668130 scopus 로고    scopus 로고
    • Determination of the sedimentation coefficient distribution by least squares boundary modeling
    • Schuck P, Rossmanith P. 2000. Determination of the sedimentation coefficient distribution by least squares boundary modeling. Biopolymers 54:328-341.
    • (2000) Biopolymers , vol.54 , pp. 328-341
    • Schuck, P.1    Rossmanith, P.2
  • 22
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultra-centrifugation: Strategies and application to model systems
    • Schuck P, Perugini MA, Gonzales NR, Howlett GJ, Schubert D. 2002. Size-distribution analysis of proteins by analytical ultra-centrifugation: Strategies and application to model systems. Biophys J 82:1096-1111.
    • (2002) Biophys J , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 23
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: A tutorial review
    • Lebowitz J, Lewis M, Schuck P. 2002. Modern analytical ultracentrifugation in protein science: A tutorial review. Protein Sci 11:2067-2079.
    • (2002) Protein Sci , vol.11 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.2    Schuck, P.3
  • 24
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S, Hippel P. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182:319-326.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.1    Hippel, P.2
  • 25
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • Harding SE, Rowe AJ, Horton JC, eds. Cambridge, UK: Royal Society of Chemistry.
    • Laue TM, Shah BD, Ridgeway TM, Pelletier SL. 1992. Computer-aided interpretation of analytical sedimentation data for proteins. In Analytical ultracentrifugation in biochemistry and polymer science; Harding SE, Rowe AJ, Horton JC, eds. Cambridge, UK: Royal Society of Chemistry: pp 90-125.
    • (1992) Analytical ultracentrifugation in biochemistry and polymer science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 26
    • 0002518285 scopus 로고    scopus 로고
    • Optical spectroscopy to characterize protein conformation and conformational changes
    • 2nd ed. New York: IRL Press
    • Schmid F. Optical spectroscopy to characterize protein conformation and conformational changes. In: Protein structure: A practical approach. 2nd ed. New York: IRL Press;1997. p. 295
    • (1997) Protein structure: A practical approach , pp. 295
    • Schmid, F.1
  • 27
    • 65349115411 scopus 로고    scopus 로고
    • Silicone microdroplets in protein formulations: Detection and enumeration
    • Sharma D, Oma P, Krishnan S. 2009. Silicone microdroplets in protein formulations: Detection and enumeration. Pharm Technol 33:74.
    • (2009) Pharm Technol , vol.33 , pp. 74
    • Sharma, D.1    Oma, P.2    Krishnan, S.3
  • 28
    • 0032078387 scopus 로고    scopus 로고
    • Application of infrared spectroscopy to development of stable lyophilized protein formulations
    • Carpenter J, Prestrelski S, Dong A. 1998. Application of infrared spectroscopy to development of stable lyophilized protein formulations. Eur J Pharm Biopharm 45:231-238.
    • (1998) Eur J Pharm Biopharm , vol.45 , pp. 231-238
    • Carpenter, J.1    Prestrelski, S.2    Dong, A.3
  • 32
    • 80054889805 scopus 로고
    • Serum albumin
    • Peters T. 1985. Serum albumin. Adv Protein Chem 178:185-188.
    • (1985) Adv Protein Chem , vol.178 , pp. 185-188
    • Peters, T.1
  • 33
    • 0036167323 scopus 로고    scopus 로고
    • A new mechanism for decreasing aggregation of recombinant human interferon-γ by a surfactant: Slowed dissolution of lyophilized formulations in a solution containing 0.03% polysorbate 20
    • Webb S, Cleland J, Carpenter J, Randolph T. 2002. A new mechanism for decreasing aggregation of recombinant human interferon-γ by a surfactant: Slowed dissolution of lyophilized formulations in a solution containing 0.03% polysorbate 20. J Pharm Sci 91:543-558.
    • (2002) J Pharm Sci , vol.91 , pp. 543-558
    • Webb, S.1    Cleland, J.2    Carpenter, J.3    Randolph, T.4
  • 35
    • 33846489611 scopus 로고    scopus 로고
    • Aggregation of recombinant human interferon alpha 2b in solution: Technical note
    • Ruiz L, Aroche K, Reyes N. 2006. Aggregation of recombinant human interferon alpha 2b in solution: Technical note. AAPS PharmSciTech 4(99):E1-5.
    • (2006) AAPS PharmSciTech , vol.4 , Issue.99
    • Ruiz, L.1    Aroche, K.2    Reyes, N.3
  • 36
    • 77949821607 scopus 로고    scopus 로고
    • Protein adsorption and excipient effects on kinetic stability of silicone oil emulsions
    • Ludwig B, Carpenter J, Hamel J, Randolph T. 2010. Protein adsorption and excipient effects on kinetic stability of silicone oil emulsions. J Pharm Sci 99(4):1721-1733.
    • (2010) J Pharm Sci , vol.99 , Issue.4 , pp. 1721-1733
    • Ludwig, B.1    Carpenter, J.2    Hamel, J.3    Randolph, T.4
  • 37
    • 0345426282 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of dimer formation and dissociation for a recombinant humanized monoclonal antibody to vascular endothelial growth factor
    • Moore J, Patapoff T, Cromwell M. 1999. Kinetics and thermodynamics of dimer formation and dissociation for a recombinant humanized monoclonal antibody to vascular endothelial growth factor. Biochemistry 38:13960-13967.
    • (1999) Biochemistry , vol.38 , pp. 13960-13967
    • Moore, J.1    Patapoff, T.2    Cromwell, M.3


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