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Volumn 102, Issue 2, 2013, Pages 429-440

Ionic strength affects tertiary structure and aggregation propensity of a monoclonal antibody adsorbed to silicone oil-water interfaces

Author keywords

Adsorption; Calorimetry (DSC); Fluorescence spectroscopy; Protein aggregation; Protein formulation; Structure

Indexed keywords

IMMUNOGLOBULIN G1 ANTIBODY; MONOCLONAL ANTIBODY; SILICONE OIL; TRYPTOPHAN; WATER;

EID: 84872490861     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23408     Document Type: Article
Times cited : (70)

References (44)
  • 1
    • 69949161060 scopus 로고    scopus 로고
    • The rise of prefilled syringes from niche product to primary container of choice: A short history
    • Romacker M, Schoenknecht T, Forster R. 2008. The rise of prefilled syringes from niche product to primary container of choice: A short history. ONdrug Deliv 4-5.
    • (2008) ONdrug Deliv , pp. 4-5
    • Romacker, M.1    Schoenknecht, T.2    Forster, R.3
  • 2
    • 45149128290 scopus 로고    scopus 로고
    • Current perspectives on stability of protein drug products during formulation, fill, and finish operations
    • Nitin R, Rajan R. 2008. Current perspectives on stability of protein drug products during formulation, fill, and finish operations. Biotechnol Prog 24:504-514.
    • (2008) Biotechnol Prog , vol.24 , pp. 504-514
    • Nitin, R.1    Rajan, R.2
  • 3
    • 0023756187 scopus 로고
    • Contamination of insulin by silicone oil: A potential hazard of plastic insulin syringes
    • Baldwin R. 1988. Contamination of insulin by silicone oil: A potential hazard of plastic insulin syringes. Diabet Med 5:789-790.
    • (1988) Diabet Med , vol.5 , pp. 789-790
    • Baldwin, R.1
  • 4
    • 0021832902 scopus 로고
    • Pollution of insulin with silicone oil, a hazard of disposable plastic syringes
    • Chantelau E, Berger M. 1985. Pollution of insulin with silicone oil, a hazard of disposable plastic syringes. Lancet 325:1459.
    • (1985) Lancet , vol.325 , pp. 1459
    • Chantelau, E.1    Berger, M.2
  • 5
    • 0023010903 scopus 로고
    • Silicone oil released from disposable insulin syringes
    • Chantelau E, Berger M, Bohlken B. 1986. Silicone oil released from disposable insulin syringes. Diabet Care 9:672-673.
    • (1986) Diabet Care , vol.9 , pp. 672-673
    • Chantelau, E.1    Berger, M.2    Bohlken, B.3
  • 6
    • 0024515587 scopus 로고
    • Silicone oil contamination of syringes
    • Chantelau E. 1989. Silicone oil contamination of syringes. Diabet Med 6:278
    • (1989) Diabet Med , vol.6 , pp. 278
    • Chantelau, E.1
  • 7
    • 0023441166 scopus 로고
    • Clouding and deactivation of clear (regular) human insulin-Association with silicone oil from disposable syringes
    • Bernstein R. 1987. Clouding and deactivation of clear (regular) human insulin-Association with silicone oil from disposable syringes. Diabet Care 10:786-787.
    • (1987) Diabet Care , vol.10 , pp. 786-787
    • Bernstein, R.1
  • 8
    • 17744363305 scopus 로고    scopus 로고
    • Silicone oil induced aggregation of proteins
    • Jones LS, Kaufmann A, Middaugh CR. 2005. Silicone oil induced aggregation of proteins. J Pharm Sci 94:918-927.
    • (2005) J Pharm Sci , vol.94 , pp. 918-927
    • Jones, L.S.1    Kaufmann, A.2    Middaugh, C.R.3
  • 10
    • 77949821607 scopus 로고    scopus 로고
    • Protein adsorption and excipient effects on kinetic stability of silicone oil emulsions
    • Ludwig DB, Carpenter JF, Hamel J-B, Randolph TW. 2010. Protein adsorption and excipient effects on kinetic stability of silicone oil emulsions. J Pharm Sci 99:1721-1733.
    • (2010) J Pharm Sci , vol.99 , pp. 1721-1733
    • Ludwig, D.B.1    Carpenter, J.F.2    Hamel, J.-B.3    Randolph, T.W.4
  • 11
    • 84885850992 scopus 로고    scopus 로고
    • US Pharmacopeia. 2011. <788> Particulate matter in injections. USP-NF, 35th ed., Rockville: US Pharmacopeia.
    • US Pharmacopeia. 2011. <788> Particulate matter in injections. USP-NF, 35th ed., Rockville: US Pharmacopeia.
  • 12
    • 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
  • 14
    • 0032809028 scopus 로고    scopus 로고
    • Adsorbed protein layers at fluid interfaces: Interactions, structure and surface rheology
    • Dickinson E. 1999. Adsorbed protein layers at fluid interfaces: Interactions, structure and surface rheology. Colloids Surf 15:161-176.
    • (1999) Colloids Surf , vol.15 , pp. 161-176
    • Dickinson, E.1
  • 15
    • 0035958458 scopus 로고    scopus 로고
    • Interfacial rheological properties of adsorbed protein layers and surfactants: A review
    • Bos MA, van Vliet T. 2001. Interfacial rheological properties of adsorbed protein layers and surfactants: A review. Adv Colloid Interface Sci 91:437-471.
    • (2001) Adv Colloid Interface Sci , vol.91 , pp. 437-471
    • Bos, M.A.1    van Vliet, T.2
  • 16
    • 17644396054 scopus 로고    scopus 로고
    • Protein stabilization of emulsions and foams
    • Damodaran S. 2005. Protein stabilization of emulsions and foams. J Food Sci 70:R54-R66.
    • (2005) J Food Sci , vol.70
    • Damodaran, S.1
  • 17
  • 18
    • 0007601535 scopus 로고
    • The adsorption of gases on plane surfaces of glass, mica and platinum
    • Langmuir I. 1918. The adsorption of gases on plane surfaces of glass, mica and platinum. J Am Chem Soc 40:1361-1403.
    • (1918) J Am Chem Soc , vol.40 , pp. 1361-1403
    • Langmuir, I.1
  • 19
    • 0018411264 scopus 로고
    • Front-face fluorometry of liquid samples
    • Eisinger J. 1979. Front-face fluorometry of liquid samples. Anal Biochem 94:15-21.
    • (1979) Anal Biochem , vol.94 , pp. 15-21
    • Eisinger, J.1
  • 21
    • 0042553279 scopus 로고
    • Smoothing and differentiation of data by simplified least squares procedures
    • Savitzky A. 1964. Smoothing and differentiation of data by simplified least squares procedures. Anal Chem 36:1627-1639.
    • (1964) Anal Chem , vol.36 , pp. 1627-1639
    • Savitzky, A.1
  • 23
    • 4444275437 scopus 로고    scopus 로고
    • Zur Lehre von der Wirkung der Salze" (about the science of the effect of salts): Franz Hofmeister's historical papers
    • Kunz W, Henle J, Ninham BW. 2004. "Zur Lehre von der Wirkung der Salze" (about the science of the effect of salts): Franz Hofmeister's historical papers. Curr Opin Colloid Interface Sci 9:19-37.
    • (2004) Curr Opin Colloid Interface Sci , vol.9 , pp. 19-37
    • Kunz, W.1    Henle, J.2    Ninham, B.W.3
  • 24
    • 0034076282 scopus 로고    scopus 로고
    • The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein
    • Vermeer A W, Norde W. 2000. The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein. Biophys J 78:394-404.
    • (2000) Biophys J , vol.78 , pp. 394-404
    • Vermeer, A.W.1    Norde, W.2
  • 25
    • 43249105327 scopus 로고    scopus 로고
    • Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies
    • Ionescu R, Vlasak J, Price C. 2008. Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies. J Pharm Sci 97:1414-1426.
    • (2008) J Pharm Sci , vol.97 , pp. 1414-1426
    • Ionescu, R.1    Vlasak, J.2    Price, C.3
  • 26
    • 33847416982 scopus 로고    scopus 로고
    • A broad range of Fab stabilities within a host of therapeutic IgGs
    • Garber E, Demarest SJ. 2007. A broad range of Fab stabilities within a host of therapeutic IgGs. Biochem Biophys Res Commun 355:751-757.
    • (2007) Biochem Biophys Res Commun , vol.355 , pp. 751-757
    • Garber, E.1    Demarest, S.J.2
  • 27
    • 0032538097 scopus 로고    scopus 로고
    • Structural changes of IgG induced by heat treatment and by adsorption onto a hydrophobic Teflon surface studied by circular dichroism spectroscopy
    • Vermeer a W, Bremer MG, Norde W. 1998. Structural changes of IgG induced by heat treatment and by adsorption onto a hydrophobic Teflon surface studied by circular dichroism spectroscopy. Biochim Biophys Acta 1425:1-12.
    • (1998) Biochim Biophys Acta , vol.1425 , pp. 1-12
    • Vermeer, A.W.1    Bremer, M.G.2    Norde, W.3
  • 28
    • 0037192769 scopus 로고    scopus 로고
    • Kinetic and structural characterization of adsorption-induced unfolding of bovine alpha-lactalbumin
    • Engel MFM, van Mierlo CPM, Visser AJWG. 2002. Kinetic and structural characterization of adsorption-induced unfolding of bovine alpha-lactalbumin. J Biol Chem 277:10922-10930.
    • (2002) J Biol Chem , vol.277 , pp. 10922-10930
    • Engel, M.F.M.1    van Mierlo, C.P.M.2    Visser, A.J.W.G.3
  • 29
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins: Intermediates and unfolded states
    • Fink AL, Calciano LJ, Goto Y, Kurotsu T, Palleros DR. 1994. Classification of acid denaturation of proteins: Intermediates and unfolded states. Biochemistry 33:12504-12511.
    • (1994) Biochemistry , vol.33 , pp. 12504-12511
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Kurotsu, T.4    Palleros, D.R.5
  • 30
    • 0023626273 scopus 로고
    • Protein folding: Hypotheses and experiments
    • Ptitsyn O. 1987. Protein folding: Hypotheses and experiments. J Protein Chem 6:273-293.
    • (1987) J Protein Chem , vol.6 , pp. 273-293
    • Ptitsyn, O.1
  • 31
    • 0018183085 scopus 로고
    • Detection and characterization of the intermediate on the folding pathway of human α-lactalbumin
    • Nozaka M, Kuwajima K, Nitta K, Sugai S. 1978. Detection and characterization of the intermediate on the folding pathway of human α-lactalbumin. Biochemistry 17:3753-3758.
    • (1978) Biochemistry , vol.17 , pp. 3753-3758
    • Nozaka, M.1    Kuwajima, K.2    Nitta, K.3    Sugai, S.4
  • 32
    • 0021114569 scopus 로고
    • Molten-globule state": A compact form of globular proteins with mobile side-chains
    • Ohgushi M, Wada A. 1983. "Molten-globule state": A compact form of globular proteins with mobile side-chains. FEBS Lett 164:21-24.
    • (1983) FEBS Lett , vol.164 , pp. 21-24
    • Ohgushi, M.1    Wada, A.2
  • 34
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi EY, Krishnan S, Randolph TW, Carpenter JF. 2003. Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation. Pharm Res 20:1325-1336.
    • (2003) Pharm Res , vol.20 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 35
    • 0026004620 scopus 로고
    • Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces
    • Sluzky V, Tamada JA, Klibanov AM, Langer R. 1991. Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces. Proc Natl Acad Sci U S A 88:9377-9381.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 9377-9381
    • Sluzky, V.1    Tamada, J.A.2    Klibanov, A.M.3    Langer, R.4
  • 36
    • 77954637757 scopus 로고    scopus 로고
    • In vitro formation of amyloid from α-synuclein is dominated by reactions at hydrophobic interfaces
    • Pronchik J, He X, Giurleo JT, Talaga DS. 2010. In vitro formation of amyloid from α-synuclein is dominated by reactions at hydrophobic interfaces. J Am Chem Soc 132:9797-9803.
    • (2010) J Am Chem Soc , vol.132 , pp. 9797-9803
    • Pronchik, J.1    He, X.2    Giurleo, J.T.3    Talaga, D.S.4
  • 37
    • 20444421544 scopus 로고    scopus 로고
    • Interpretation of protein adsorption: Surface-induced conformational changes
    • Roach P, Farrar D, Perry CC. 2005. Interpretation of protein adsorption: Surface-induced conformational changes. J Am Chem Soc 127:8168-8173.
    • (2005) J Am Chem Soc , vol.127 , pp. 8168-8173
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 38
    • 21244462685 scopus 로고    scopus 로고
    • Protein structural perturbation and aggregation on homogeneous surfaces
    • Sethuraman A, Belfort G. 2005. Protein structural perturbation and aggregation on homogeneous surfaces. Biophys J 88:1322-1333.
    • (2005) Biophys J , vol.88 , pp. 1322-1333
    • Sethuraman, A.1    Belfort, G.2
  • 39
    • 80054986127 scopus 로고    scopus 로고
    • Conformational changes to deamidated wheat gliadins and β-casein upon adsorption to oil-water emulsion interfaces
    • Wong BT, Zhai J, Hoffmann SV, Aguilar M-I, Augustin M, Wooster TJ, Day L. 2012. Conformational changes to deamidated wheat gliadins and β-casein upon adsorption to oil-water emulsion interfaces. Food Hydrocolloids 27:91-101.
    • (2012) Food Hydrocolloids , vol.27 , pp. 91-101
    • Wong, B.T.1    Zhai, J.2    Hoffmann, S.V.3    Aguilar, M.-I.4    Augustin, M.5    Wooster, T.J.6    Day, L.7
  • 40
    • 79960770032 scopus 로고    scopus 로고
    • Structural rearrangement of β-lactoglobulin at different oil-water interfaces and its effect on emulsion stability
    • Zhai J, Wooster TJ, Hoffmann SV, Lee T-H, Augustin MA, Aguilar M-I. 2011. Structural rearrangement of β-lactoglobulin at different oil-water interfaces and its effect on emulsion stability. Langmuir 27:9227-9236.
    • (2011) Langmuir , vol.27 , pp. 9227-9236
    • Zhai, J.1    Wooster, T.J.2    Hoffmann, S.V.3    Lee, T.-H.4    Augustin, M.A.5    Aguilar, M.-I.6
  • 41
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • Roberts C. 2007. Non-native protein aggregation kinetics. Biotechnol Bioeng 98:927-938.
    • (2007) Biotechnol Bioeng , vol.98 , pp. 927-938
    • Roberts, C.1
  • 42
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • Uversky VN, Fink AL. 2004. Conformational constraints for amyloid fibrillation: The importance of being unfolded. Biochim Biophys Acta 1698:131-153.
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 43
    • 0242515822 scopus 로고    scopus 로고
    • Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor
    • Chi E, Krishnan S, Kendrick B. 2003. Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Protein Sci 12:903-913.
    • (2003) Protein Sci , vol.12 , pp. 903-913
    • Chi, E.1    Krishnan, S.2    Kendrick, B.3
  • 44
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • Lumry R. 1954. Conformation changes of proteins. J Phys Chem 58:110-120.
    • (1954) J Phys Chem , vol.58 , pp. 110-120
    • Lumry, R.1


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