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Volumn 95, Issue 9, 2006, Pages 1967-1983

Application of high-frequency rheology measurements for analyzing protein-protein interactions in high protein concentration solutions using a model monoclonal antibody (IgG2)

Author keywords

complex viscosity; High protein concentration solutions; IgG2; Monoclonal antibody; Protein; Protein formulation; Protein protein interactions; Stability; Storage modulus; Ultrasonic shear rheometer

Indexed keywords

IMMUNOGLOBULIN G2; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY IMMUNOGLOBULIN G2; MONOMER; UNCLASSIFIED DRUG;

EID: 33748937041     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.20663     Document Type: Article
Times cited : (55)

References (54)
  • 1
    • 0031768735 scopus 로고    scopus 로고
    • Protein interactions in solution characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen
    • Velev OD, Kaler EW, Lenhoff AM. 1998. Protein interactions in solution characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen. Biophys J 75:2682-2697.
    • (1998) Biophys J , vol.75 , pp. 2682-2697
    • Velev, O.D.1    Kaler, E.W.2    Lenhoff, A.M.3
  • 2
    • 0032484699 scopus 로고    scopus 로고
    • Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes
    • Curtis RA, Prausnitz JM, Blanch HW. 1998. Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes. Biotechnol Bioeng 57:11-21.
    • (1998) Biotechnol Bioeng , vol.57 , pp. 11-21
    • Curtis, R.A.1    Prausnitz, J.M.2    Blanch, H.W.3
  • 3
    • 0030571043 scopus 로고    scopus 로고
    • Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions
    • Wen J, Arakawa T, Philo JS. 1996. Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal Biochem 240:155-166.
    • (1996) Anal Biochem , vol.240 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 4
    • 11844292073 scopus 로고    scopus 로고
    • New methods for measuring macromolecular interactions in solution via static light scatering: Basic methodology and application to nonassociating and self-associating proteins
    • Attri AK, Minton AP. 2005. New methods for measuring macromolecular interactions in solution via static light scatering: Basic methodology and application to nonassociating and self-associating proteins. Anal Biochem 337:103-110.
    • (2005) Anal Biochem , vol.337 , pp. 103-110
    • Attri, A.K.1    Minton, A.P.2
  • 5
    • 0037378389 scopus 로고    scopus 로고
    • The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient
    • Ho JGS, Middelberg APJ, Ramage P, Kocher HP. 2003. The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient. Protein Sci 12:708-716.
    • (2003) Protein Sci , vol.12 , pp. 708-716
    • Ho, J.G.S.1    Middelberg, A.P.J.2    Ramage, P.3    Kocher, H.P.4
  • 6
    • 0030566439 scopus 로고    scopus 로고
    • Protein interaction and crystallization
    • Rosenbaum DF, Zukoski CF. 1996. Protein interaction and crystallization. J Cryst Growth 169:752-758.
    • (1996) J Cryst Growth , vol.169 , pp. 752-758
    • Rosenbaum, D.F.1    Zukoski, C.F.2
  • 7
    • 10044279535 scopus 로고    scopus 로고
    • Determination of second virial coefficient of proteins using a dual-detector cell for simultaneous measurement of scattered light intensity and concentration in SEC-HPLC
    • Bajaj H, Sharma VK, Kalonia DS. 2004. Determination of second virial coefficient of proteins using a dual-detector cell for simultaneous measurement of scattered light intensity and concentration in SEC-HPLC. Biophys J 87:4048-4055.
    • (2004) Biophys J , vol.87 , pp. 4048-4055
    • Bajaj, H.1    Sharma, V.K.2    Kalonia, D.S.3
  • 9
    • 1642578812 scopus 로고    scopus 로고
    • Thermodynamic properties of supersaturated protein solutions
    • Knezic D, Zaccaro J, Myerson AS. 2004. Thermodynamic properties of supersaturated protein solutions. Crystal Growth Des 4:199-208.
    • (2004) Crystal Growth Des , vol.4 , pp. 199-208
    • Knezic, D.1    Zaccaro, J.2    Myerson, A.S.3
  • 10
    • 0348207551 scopus 로고    scopus 로고
    • Effect of protein-protein interactions on protein aggregation kinetics
    • Zhang J, Liu XY. 2003. Effect of protein-protein interactions on protein aggregation kinetics. J Chem Phys 119:10972-10976.
    • (2003) J Chem Phys , vol.119 , pp. 10972-10976
    • Zhang, J.1    Liu, X.Y.2
  • 11
    • 1942473133 scopus 로고    scopus 로고
    • Direct measurement of protein osmotic second virial cross coefficient by cross-interaction chromatography
    • Tessier PM, Sandler SI, Lenhoff AM. 2004. Direct measurement of protein osmotic second virial cross coefficient by cross-interaction chromatography. Protein Sci 13:1379-1390.
    • (2004) Protein Sci , vol.13 , pp. 1379-1390
    • Tessier, P.M.1    Sandler, S.I.2    Lenhoff, A.M.3
  • 12
    • 25444487734 scopus 로고    scopus 로고
    • Influence of macromolecular crowding upon the stability and state of association of proteins: Predictions and observations
    • Minton AP. 2005. Influence of macromolecular crowding upon the stability and state of association of proteins: Predictions and observations. J Pharma Sci 94:1668-1675.
    • (2005) J Pharma Sci , vol.94 , pp. 1668-1675
    • Minton, A.P.1
  • 14
    • 33748950545 scopus 로고
    • Viscosity of dilute solutions of long-chain molecules. V. Dependence on the solvent
    • Huggins ML. 1943. Viscosity of dilute solutions of long-chain molecules. V. Dependence on the solvent. J Appl Phys 14:246-248.
    • (1943) J Appl Phys , vol.14 , pp. 246-248
    • Huggins, M.L.1
  • 16
    • 3843058933 scopus 로고    scopus 로고
    • Commercial manufacturing scale formulation and analytical characterization of therapeutic recombinant antibodies
    • Harris RJ, Shire SJ, Winter C. 2004. Commercial manufacturing scale formulation and analytical characterization of therapeutic recombinant antibodies. Drug Dev Res 61:137-154.
    • (2004) Drug Dev Res , vol.61 , pp. 137-154
    • Harris, R.J.1    Shire, S.J.2    Winter, C.3
  • 17
    • 34249290252 scopus 로고
    • The viscosity of a concentrated suspension of spherical particles
    • Mooney M. 1951. The viscosity of a concentrated suspension of spherical particles. J Colloid Sci 6:162-170.
    • (1951) J Colloid Sci , vol.6 , pp. 162-170
    • Mooney, M.1
  • 18
    • 0000505523 scopus 로고
    • Modeling biological macromolecules in solution: 1. The ellipsoid of revolution
    • Harding SE, Rowe AJ. 1982. Modeling biological macromolecules in solution: 1. The ellipsoid of revolution. Int J Biol Macromol 4:160-164.
    • (1982) Int J Biol Macromol , vol.4 , pp. 160-164
    • Harding, S.E.1    Rowe, A.J.2
  • 19
    • 0020668187 scopus 로고
    • The effect of volume occupancy upon the thermodynamic activity of proteins: Some biochemical consequences
    • Minton AP. 1983. The effect of volume occupancy upon the thermodynamic activity of proteins: Some biochemical consequences. Mol Cell Biochem 55:119-140.
    • (1983) Mol Cell Biochem , vol.55 , pp. 119-140
    • Minton, A.P.1
  • 20
    • 27644477360 scopus 로고    scopus 로고
    • Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution
    • Liu J, Nguyen MDH, Andya JD, Shire SJ. 2005. Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution. J Pharm Sci 94:1928-1940.
    • (2005) J Pharm Sci , vol.94 , pp. 1928-1940
    • Liu, J.1    Nguyen, M.D.H.2    Andya, J.D.3    Shire, S.J.4
  • 21
    • 0037028161 scopus 로고    scopus 로고
    • Biological water: Femtosecond dynamics of macromolecular hydration
    • Pal SK, Peon J, Bagchi B, Zewail AH. 2002. Biological water: femtosecond dynamics of macromolecular hydration. J Phys Chem B 106:12376-12395.
    • (2002) J Phys Chem B , vol.106 , pp. 12376-12395
    • Pal, S.K.1    Peon, J.2    Bagchi, B.3    Zewail, A.H.4
  • 22
    • 0034049350 scopus 로고    scopus 로고
    • Kinetics of desolvation-mediated protein-protein binding
    • Camacho CJ, Kimura SR, DeLisi C, Vajda S. 2000. Kinetics of desolvation-mediated protein-protein binding. Biophys J 78:1094-1105.
    • (2000) Biophys J , vol.78 , pp. 1094-1105
    • Camacho, C.J.1    Kimura, S.R.2    DeLisi, C.3    Vajda, S.4
  • 23
    • 0035256906 scopus 로고    scopus 로고
    • Monitoring of acidified milk gel formation by ultrasonic shear wave measurements. High-frequency viscoelastic moduli of milk and acidified milk gel
    • Kudryashov ED, Hunt NT, Arikainen EO, Buckin VA. 2001. Monitoring of acidified milk gel formation by ultrasonic shear wave measurements. High-frequency viscoelastic moduli of milk and acidified milk gel. J Dairy Sci 84:375-388.
    • (2001) J Dairy Sci , vol.84 , pp. 375-388
    • Kudryashov, E.D.1    Hunt, N.T.2    Arikainen, E.O.3    Buckin, V.A.4
  • 24
    • 0034746683 scopus 로고    scopus 로고
    • Ultrasonic shear wave rheology of weak particle gels
    • Buckin V, Kudryashov E. 2001. Ultrasonic shear wave rheology of weak particle gels. Adv Colloid Interface Sci 89-90:401-422.
    • (2001) Adv Colloid Interface Sci , vol.89-90 , pp. 401-422
    • Buckin, V.1    Kudryashov, E.2
  • 25
    • 0010329713 scopus 로고
    • The nature of viscoelastic behavior
    • Ferry JD, editor. New York: John Wiley & Sons
    • Ferry JD. 1962. The nature of viscoelastic behavior. In: Ferry JD, editor. Viscoelastic properties of polymers. New York: John Wiley & Sons, pp 1-40.
    • (1962) Viscoelastic Properties of Polymers , pp. 1-40
    • Ferry, J.D.1
  • 27
    • 21344472449 scopus 로고    scopus 로고
    • Measurement of fluid viscosity at microliter volumes using quartz impedance analysis
    • Article 47
    • Saluja A, Kalonia DS. 2004. Measurement of fluid viscosity at microliter volumes using quartz impedance analysis. AAPS Pharm Sci Tech 5: (Article 47).
    • (2004) AAPS Pharm Sci Tech , vol.5
    • Saluja, A.1    Kalonia, D.S.2
  • 28
    • 21344457192 scopus 로고    scopus 로고
    • The application of ultrasonic shear rheometer to characterize rheological properties of high protein concentration solutions at microliter volume
    • Saluja A, Kalonia DS. 2005. The application of ultrasonic shear rheometer to characterize rheological properties of high protein concentration solutions at microliter volume. J Pharm Sci 94:1161-1168.
    • (2005) J Pharm Sci , vol.94 , pp. 1161-1168
    • Saluja, A.1    Kalonia, D.S.2
  • 29
    • 33748944254 scopus 로고
    • Experimental methods for viscoelastic liquids
    • Ferry JD, editor. New York: John Wiley & Sons
    • Ferry JD. 1961. Experimental methods for viscoelastic liquids. In: Ferry JD, editor. Viscoelastic properties of polymers. New York: John Wiley & Sons, pp 82-104.
    • (1961) Viscoelastic Properties of Polymers , pp. 82-104
    • Ferry, J.D.1
  • 30
    • 33748939678 scopus 로고
    • Solvent effects on emission spectra
    • Creighton TE, editor. New York: W.H. Freeman and Company
    • Creighton TE. 1993. Solvent effects on emission spectra. In: Creighton TE, editor. Proteins: Structures and molecular properties, 2nd ed. New York: W.H. Freeman and Company, pp 185-210.
    • (1993) Proteins: Structures and Molecular Properties, 2nd Ed. , pp. 185-210
    • Creighton, T.E.1
  • 31
    • 0034001548 scopus 로고    scopus 로고
    • Comparison of protein surface hydrophobicity measured at various pH using three different fluorescent probes
    • Alizadeh-Pasdar N, Li-Chan ECY. 2000. Comparison of protein surface hydrophobicity measured at various pH using three different fluorescent probes. J Agric Food Chem 48:328-334.
    • (2000) J Agric Food Chem , vol.48 , pp. 328-334
    • Alizadeh-Pasdar, N.1    Li-Chan, E.C.Y.2
  • 32
    • 0035019184 scopus 로고    scopus 로고
    • Application of prodan fluorescent probe to measure surface hydrophobicity of proteins interacting with k-carrageenan
    • Alizadeh-Pasdar N, Li-Chan ECY. 2001. Application of prodan fluorescent probe to measure surface hydrophobicity of proteins interacting with k-carrageenan. Food Hydrocolloids 15:285-294.
    • (2001) Food Hydrocolloids , vol.15 , pp. 285-294
    • Alizadeh-Pasdar, N.1    Li-Chan, E.C.Y.2
  • 33
    • 0001296380 scopus 로고    scopus 로고
    • Hydrophobicity of bovine serum albumin and ovalbumin determined using uncharged (prodan) and anionic (ANS-) fluorescent probes
    • Haskard CA, Li-Chan ECY. 1998. Hydrophobicity of bovine serum albumin and ovalbumin determined using uncharged (prodan) and anionic (ANS-) fluorescent probes. J Agric Food Chem 46:2671-2677.
    • (1998) J Agric Food Chem , vol.46 , pp. 2671-2677
    • Haskard, C.A.1    Li-Chan, E.C.Y.2
  • 34
    • 0033049201 scopus 로고    scopus 로고
    • Evidence of heterogenous 1-anilinonaphthalene-8-sulfonate binding to b-lactoglobulin from fluorescence spectroscopy
    • D'Alfonso L, Collini M, Baldini G. 1999. Evidence of heterogenous 1-anilinonaphthalene-8-sulfonate binding to b-lactoglobulin from fluorescence spectroscopy. Biochim Biophys Acta 1432:194-202.
    • (1999) Biochim Biophys Acta , vol.1432 , pp. 194-202
    • D'Alfonso, L.1    Collini, M.2    Baldini, G.3
  • 36
    • 0002112253 scopus 로고    scopus 로고
    • Gelation of globular proteins
    • Hill SE, Ledward DA, Mitchell JR, editor. Gaithersburg, Maryland: Aspen
    • Clark AH. 1998. Gelation of Globular Proteins. In: Hill SE, Ledward DA, Mitchell JR, editor. Functional properties of food macromolecules, 2nd ed. Gaithersburg, Maryland: Aspen, pp 77-142.
    • (1998) Functional Properties of Food Macromolecules, 2nd Ed. , pp. 77-142
    • Clark, A.H.1
  • 38
    • 0017397771 scopus 로고
    • Hard quasispherical model for the viscosity of hemoglobin solutions
    • Ross PD, Minton AP. 1977. Hard quasispherical model for the viscosity of hemoglobin solutions. Biochem Biophys Res Commun 76:971-976.
    • (1977) Biochem Biophys Res Commun , vol.76 , pp. 971-976
    • Ross, P.D.1    Minton, A.P.2
  • 39
    • 0002338415 scopus 로고    scopus 로고
    • Proteins at liquid interfaces
    • Baszkin A, Norde W, editors. New York: Marcel Dekker
    • Norde W. 2000. Proteins at liquid interfaces. In: Baszkin A, Norde W, editors. Physical chemistry of biological interfaces. New York: Marcel Dekker, pp 115-136.
    • (2000) Physical Chemistry of Biological Interfaces , pp. 115-136
    • Norde, W.1
  • 41
    • 0000864899 scopus 로고
    • Adsorption of proteins onto polymeric surfaces of different hydrophilicities - A case study with bovine serum albumin
    • Lee SH, Ruckenstein E. 1988. Adsorption of proteins onto polymeric surfaces of different hydrophilicities - a case study with bovine serum albumin. J Colloid Interface Sci 125:365-379.
    • (1988) J Colloid Interface Sci , vol.125 , pp. 365-379
    • Lee, S.H.1    Ruckenstein, E.2
  • 42
    • 0025700708 scopus 로고
    • Thermodynamic non-ideality in macromolecular solutions
    • Shearwin KE, Winzor DJ. 1990. Thermodynamic non-ideality in macromolecular solutions. Eur J Biochem 190:523-529.
    • (1990) Eur J Biochem , vol.190 , pp. 523-529
    • Shearwin, K.E.1    Winzor, D.J.2
  • 44
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • Minton AP. 2000. Implications of macromolecular crowding for protein assembly. Curr Opin Struct Biol 10:34-39.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 45
    • 16344364032 scopus 로고    scopus 로고
    • Models for excluded volume interaction between an unfolded protein and rigid macromolecular cosolutes: Macromolecular crowding and protein stability revisited
    • Minton AP. 2005. Models for excluded volume interaction between an unfolded protein and rigid macromolecular cosolutes: Macromolecular crowding and protein stability revisited. Biophys J 88:971-985.
    • (2005) Biophys J , vol.88 , pp. 971-985
    • Minton, A.P.1
  • 46
    • 0001857899 scopus 로고    scopus 로고
    • Thermodynamics of protein adsorption
    • Brash JL, Wojciechowski PW, editors. New York: Marcel Dekker
    • Norde W, Haynes CA. 1996. Thermodynamics of protein adsorption. In: Brash JL, Wojciechowski PW, editors. Interfacial phenomenon and bioproducts. New York: Marcel Dekker, pp 123-144.
    • (1996) Interfacial Phenomenon and Bioproducts , pp. 123-144
    • Norde, W.1    Haynes, C.A.2
  • 47
    • 0035142983 scopus 로고    scopus 로고
    • Calculation of weak protein-protein interactions: The pH dependence of the second virial coefficient
    • Elcock AH, McCammon JA. 2001. Calculation of weak protein-protein interactions: The pH dependence of the second virial coefficient. Biophys J 80:613-625.
    • (2001) Biophys J , vol.80 , pp. 613-625
    • Elcock, A.H.1    McCammon, J.A.2
  • 48
    • 11744320872 scopus 로고
    • The viscosity of aqueous solutions of bovine serum albumin between pH 4.3 and 10.5
    • Tanford C, Buzzell JG. 1956. The viscosity of aqueous solutions of bovine serum albumin between pH 4.3 and 10.5. J Phys Chem 60:225-231.
    • (1956) J Phys Chem , vol.60 , pp. 225-231
    • Tanford, C.1    Buzzell, J.G.2
  • 49
    • 0142073964 scopus 로고    scopus 로고
    • Dilute solution viscometry of food biopolymers
    • Hill SE, Ledward DA, Mitchell JR, editors. Gaithersburg, Maryland: Aspen
    • Harding SE. 1998. Dilute solution viscometry of food biopolymers. In: Hill SE, Ledward DA, Mitchell JR, editors. Functional properties of food macromolecules, 2nd ed. Gaithersburg, Maryland: Aspen, pp 77-142.
    • (1998) Functional Properties of Food Macromolecules, 2nd Ed. , pp. 77-142
    • Harding, S.E.1
  • 50
    • 0013601141 scopus 로고
    • Nuclear magnetic resonance studies of chloride binding to proteins
    • Bull T, Norne JE, Reimarsson P, Lindman B. 1978. Nuclear magnetic resonance studies of chloride binding to proteins. J Am Chem Soc 100:4643-4647.
    • (1978) J Am Chem Soc , vol.100 , pp. 4643-4647
    • Bull, T.1    Norne, J.E.2    Reimarsson, P.3    Lindman, B.4
  • 51
    • 0000513877 scopus 로고
    • A study of the binding of small ions in protein solutions with the use of membrane electrodes. I. The binding of the chloride ion and other inorganic anions in solutions of serum albumin
    • Carr CW. 1952. A study of the binding of small ions in protein solutions with the use of membrane electrodes. I. The binding of the chloride ion and other inorganic anions in solutions of serum albumin. Arch Biochem Biophys 40:286-294.
    • (1952) Arch Biochem Biophys , vol.40 , pp. 286-294
    • Carr, C.W.1
  • 52
    • 0142122294 scopus 로고    scopus 로고
    • Measurements of protein self-association as a guide to crystallization
    • Tessier PM, Lenhoff AM. 2003. Measurements of protein self-association as a guide to crystallization. Curr Opin Biotechnol 14:512-516.
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 512-516
    • Tessier, P.M.1    Lenhoff, A.M.2
  • 54
    • 2442764929 scopus 로고
    • Capillary electrophoresis of proteins
    • Herron JN, Jiskoot W, Crommelin DJA, editors. New York: Plenum press
    • van de Goor TA. 1995. Capillary electrophoresis of proteins. In: Herron JN, Jiskoot W, Crommelin DJA, editors. Physical methods to characterize pharmaceutical proteins. New York: Plenum press.
    • (1995) Physical Methods to Characterize Pharmaceutical Proteins
    • Van De Goor, T.A.1


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