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Volumn 19, Issue 2, 2010, Pages 279-290

Aggregation of a multidomain protein: A coagulation mechanism governs aggregation of a model IgG1 antibody under weak thermal stress

Author keywords

Coagulation; Dynamic light scattering; Monoclonal IgG1 antibody; Multidomain; Protein aggregation; Rituximab; Tween 80

Indexed keywords

IMMUNOGLOBULIN G1;

EID: 76749130326     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.309     Document Type: Article
Times cited : (70)

References (57)
  • 1
    • 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
  • 2
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM (2003) Protein folding and misfolding. Nature 426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 4
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: A formulation challenge
    • Frokjaer S, Otzen DE (2005) Protein drug stability: a formulation challenge. Nat Rev Drug Discov 4:298-306.
    • (2005) Nat Rev Drug Discov , vol.4 , pp. 298-306
    • Frokjaer, S.1    Otzen, D.E.2
  • 6
    • 33845940104 scopus 로고    scopus 로고
    • Real-time and single fibril observation of the formation of amyloid β spherulitic structures
    • Ban T, Morigaki K, Yagi H, Kawasaki T, Kobayashi A, Yuba S, Naiki H, Goto Y (2006) Real-time and single fibril observation of the formation of amyloid β spherulitic structures. J Biol Chem 281:33677-33683.
    • (2006) J Biol Chem , vol.281 , pp. 33677-33683
    • Ban, T.1    Morigaki, K.2    Yagi, H.3    Kawasaki, T.4    Kobayashi, A.5    Yuba, S.6    Naiki, H.7    Goto, Y.8
  • 7
    • 30744469843 scopus 로고    scopus 로고
    • Solvation-assisted pressure tuning of insulin fibrillation: From novel aggregation pathways to biotechnological applications
    • Grudzielanek S, Smirnovas V, Winter R (2006) Solvation-assisted pressure tuning of insulin fibrillation: from novel aggregation pathways to biotechnological applications. J Mol Biol 356:497-509.
    • (2006) J Mol Biol , vol.356 , pp. 497-509
    • Grudzielanek, S.1    Smirnovas, V.2    Winter, R.3
  • 8
    • 33846839238 scopus 로고    scopus 로고
    • Protein particulates: Another generic form of protein aggregation?
    • Krebs MR, Devlin GL, Donald A (2005) Protein particulates: another generic form of protein aggregation? Biophys J 92:1336-1342.
    • (2005) Biophys J , vol.92 , pp. 1336-1342
    • Krebs, M.R.1    Devlin, G.L.2    Donald, A.3
  • 9
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants
    • Lomakin A, Chung DS, Benedek GB, Kirschner DA, Teplow DB (1996) On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants. Proc Natl Acad Sci USA 93: 1125-1129.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 11
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • Roberts CJ (2007) Non-native protein aggregation kinetics. Biotechnol Bioeng 98:927-938.
    • (2007) Biotechnol Bioeng , vol.98 , pp. 927-938
    • Roberts, C.J.1
  • 12
    • 0032564420 scopus 로고    scopus 로고
    • A transient expansion of the native state precedes aggregation of recombinant human interferon-γ
    • Kendrick BS, Carpenter JF, Cleland JL, Randolph TW (1998) A transient expansion of the native state precedes aggregation of recombinant human interferon-γ. Proc Natl Acad Sci USA 95:14142-14146.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14142-14146
    • Kendrick, B.S.1    Carpenter, J.F.2    Cleland, J.L.3    Randolph, T.W.4
  • 14
    • 29244462955 scopus 로고    scopus 로고
    • Structural characterization and immunogenicity in wild-type and immune tolerant mice of degraded recombinant human interferon alpha2b
    • Hermeling S, Aranha L, Damen JMA, Slijper M, Schellekens H, Crommelin DJA, Jiskoot W (2005) Structural characterization and immunogenicity in wild-type and immune tolerant mice of degraded recombinant human interferon alpha2b. Pharm Res 22:1997-2006.
    • (2005) Pharm Res , vol.22 , pp. 1997-2006
    • Hermeling, S.1    Aranha, L.2    Damen, J.M.A.3    Slijper, M.4    Schellekens, H.5    Crommelin, D.J.A.6    Jiskoot, W.7
  • 15
    • 36049006592 scopus 로고    scopus 로고
    • Immunogenicity of protein therapeutics
    • De Groot AS, Scott DW (2007) Immunogenicity of protein therapeutics. Trends Immunol 28:482-490.
    • (2007) Trends Immunol , vol.28 , pp. 482-490
    • De Groot, A.S.1    Scott, D.W.2
  • 16
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An immunologic perspective
    • Rosenberg AS (2006) Effects of protein aggregates: an immunologic perspective. AAPS J 8:E501-E507.
    • (2006) AAPS , vol.J 8
    • Rosenberg, A.S.1
  • 17
    • 7244248664 scopus 로고    scopus 로고
    • From the bench to the bedside: Ways to improve rituximab efficacy
    • Cartron G, Watier H, Golay J, Solal-Celigny P (2004) From the bench to the bedside: ways to improve rituximab efficacy. Blood 104:2635-2642.
    • (2004) Blood , vol.104 , pp. 2635-2642
    • Cartron, G.1    Watier, H.2    Golay, J.3    Solal-Celigny, P.4
  • 18
    • 0000722759 scopus 로고
    • Scaling behavior and cluster fractal dimension determined by light scattering from aggregating proteins
    • Feder J, Jøssang T, Rosenqvist E (1984) Scaling behavior and cluster fractal dimension determined by light scattering from aggregating proteins. Phys Rev Lett 53:1403-1406.
    • (1984) Phys Rev Lett , vol.53 , pp. 1403-1406
    • Feder, J.1    Jøssang, T.2    Rosenqvist, E.3
  • 19
  • 20
    • 55749109195 scopus 로고    scopus 로고
    • Shaken, not stirred: Mechanical stress testing of an IgG1 antibody
    • Kiese S, Papppenberger A, Friess W, Mahler H-C (2008) Shaken, not stirred: mechanical stress testing of an IgG1 antibody. J Pharm Sci 97:4347-4366.
    • (2008) J Pharm Sci , vol.97 , pp. 4347-4366
    • Kiese, S.1    Papppenberger, A.2    Friess, W.3    Mahler, H.-C.4
  • 23
    • 0022999364 scopus 로고
    • Characterization of a heat-stable fraction of human IgG
    • Rosenqvist E, Jøssang T, Feder J, Harbitz O (1986) Characterization of a heat-stable fraction of human IgG. J Prot Chem 5:323-333.
    • (1986) J Prot Chem , vol.5 , pp. 323-333
    • Rosenqvist, E.1    Jøssang, T.2    Feder, J.3    Harbitz, O.4
  • 24
    • 68949122431 scopus 로고    scopus 로고
    • Elucidation of two major aggregation pathways in an IgG2 antibody
    • Van Buren N, Rehder D, Gadgil H, Matsumura M, Jacob J (2009) Elucidation of two major aggregation pathways in an IgG2 antibody. J Pharm Sci 98:3013-3030.
    • (2009) J Pharm Sci , vol.98 , pp. 3013-3030
    • Van Buren, N.1    Rehder, D.2    Gadgil, H.3    Matsumura, M.4    Jacob, J.5
  • 25
    • 70349646469 scopus 로고    scopus 로고
    • Characterization of high-molecular-weight nonnative aggregates and aggregation kinetics by size exclusion chromatography with inline multi-angle laser light scattering
    • Li Y, Weiss WF, IV, Roberts CJ (2009) Characterization of high-molecular-weight nonnative aggregates and aggregation kinetics by size exclusion chromatography with inline multi-angle laser light scattering. J Pharm Sci 98:3997-4017.
    • (2009) J Pharm Sci , vol.98 , pp. 3997-4017
    • Li, Y.1    Weiss2    WF, I.V.3    Roberts, C.J.4
  • 26
    • 0033898830 scopus 로고    scopus 로고
    • Characterization and isolation of intermediates in β-lactoglobulin heat aggregation at high pH
    • Bauer R, Carrotta R, Rischel C, Øgendahl L (2000) Characterization and isolation of intermediates in β-lactoglobulin heat aggregation at high pH. Biophys J 79:1030-1038.
    • (2000) Biophys J , vol.79 , pp. 1030-1038
    • Bauer, R.1    Carrotta, R.2    Rischel, C.3    Øgendahl, L.4
  • 27
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone F (1999) Analysis of protein aggregation kinetics. Methods Enzymol 309:256-274.
    • (1999) Methods Enzymol , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 28
    • 37549031260 scopus 로고    scopus 로고
    • Amyloid - a state in many guises: Survival of the fittest fibril fold
    • Pedersen JS, Otzen DE (2008) Amyloid - a state in many guises: survival of the fittest fibril fold. Protein Sci 17:2-10.
    • (2008) Protein Sci , vol.17 , pp. 2-10
    • Pedersen, J.S.1    Otzen, D.E.2
  • 29
    • 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
  • 30
    • 43249105327 scopus 로고    scopus 로고
    • Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies
    • Ionescu RM, Vlasak J, Price C, Kirchmeier M (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.M.1    Vlasak, J.2    Price, C.3    Kirchmeier, M.4
  • 31
    • 50249132634 scopus 로고    scopus 로고
    • Antibody therapeutics, antibody engineering, and the merits of protein stability
    • Demarest S, Glaser S (2008) Antibody therapeutics, antibody engineering, and the merits of protein stability. Curr Opin Drug Discov Dev 11:675-687.
    • (2008) Curr Opin Drug Discov Dev , vol.11 , pp. 675-687
    • Demarest, S.1    Glaser, S.2
  • 32
    • 0026586591 scopus 로고
    • Thereotical analysis of Lumry-Eyring models in differential scanning calorimetry
    • Sánchez-Ruiz JM (1992) Thereotical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys J 61:921-935.
    • (1992) Biophys J , vol.61 , pp. 921-935
    • Sánchez-Ruiz, J.M.1
  • 33
    • 0034076282 scopus 로고    scopus 로고
    • The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein
    • Vermeer AWP, 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.P.1    Norde, W.2
  • 34
    • 0029203156 scopus 로고
    • Differential scanning calorimetry of proteins
    • Sánchez-Ruiz JM (1995) Differential scanning calorimetry of proteins. Subcell Biochem 24:133-176.
    • (1995) Subcell Biochem , vol.24 , pp. 133-176
    • Sánchez-Ruiz, J.M.1
  • 35
    • 0024281290 scopus 로고
    • Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin
    • Sánchez-Ruiz JM, López-Lacomba JL, Cortijo M, Mateo PL (1988) Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin. Biochemistry 27:1648-1652.
    • (1988) Biochemistry , vol.27 , pp. 1648-1652
    • Sánchez-Ruiz, J.M.1    López-Lacomba, J.L.2    Cortijo, M.3    Mateo, P.L.4
  • 36
    • 33947544337 scopus 로고    scopus 로고
    • Highly concentrated monoclonal antibody solutions: Direct analysis of physical structure and thermal stability
    • Harn N, Allan C, Oliver C, Middaugh CR (2007) Highly concentrated monoclonal antibody solutions: direct analysis of physical structure and thermal stability. J Pharm Sci 96:532-546.
    • (2007) J Pharm Sci , vol.96 , pp. 532-546
    • Harn, N.1    Allan, C.2    Oliver, C.3    Middaugh, C.R.4
  • 37
    • 36049057066 scopus 로고
    • Theory of critical-point scattering and correlations. I. The Ising model
    • Fisher ME, Burford RJ (1967) Theory of critical-point scattering and correlations. I. The Ising model. Phys Rev 156:583-622.
    • (1967) Phys Rev , vol.156 , pp. 583-622
    • Fisher, M.E.1    Burford, R.J.2
  • 38
    • 0028195932 scopus 로고
    • Structure and distribution of aggregates formed after heat-induced denaturation of globular proteins
    • Gimel JC, Durand D, Nicolai T (1994) Structure and distribution of aggregates formed after heat-induced denaturation of globular proteins. Macromolecules 27:583-589.
    • (1994) Macromolecules , vol.27 , pp. 583-589
    • Gimel, J.C.1    Durand, D.2    Nicolai, T.3
  • 39
    • 0001386179 scopus 로고    scopus 로고
    • Analysis of aggregate structure in food protein gels with the concept of fractal
    • Hagiwara T, Kumagai H, Matsunaga T, Nakamura K (1998) Analysis of aggregate structure in food protein gels with the concept of fractal. Biosci Biotechnol Biochem 61:1663-1667.
    • (1998) Biosci Biotechnol Biochem , vol.61 , pp. 1663-1667
    • Hagiwara, T.1    Kumagai, H.2    Matsunaga, T.3    Nakamura, K.4
  • 40
    • 24044518189 scopus 로고    scopus 로고
    • Protofibril formation of amyloid β-protein at low pH via a non-cooperative elongation mechanism
    • Carrotta R, Manno M, Bulone D, Martorana V, San Biagio PL (2005) Protofibril formation of amyloid β-protein at low pH via a non-cooperative elongation mechanism. J Biol Chem 280:30001-30008.
    • (2005) J Biol Chem , vol.280 , pp. 30001-30008
    • Carrotta, R.1    Manno, M.2    Bulone, D.3    Martorana, V.4    San Biagio, P.L.5
  • 41
    • 0342374989 scopus 로고    scopus 로고
    • Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation
    • Le Bon C, Nicolai T, Durand D (1999) Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation. Macromolecules 32:6120-6127.
    • (1999) Macromolecules , vol.32 , pp. 6120-6127
    • Le Bon, C.1    Nicolai, T.2    Durand, D.3
  • 43
    • 35949010320 scopus 로고
    • Variable aggregation rates in colloidal gold: Kernel homogeneity dependence on aggregant concentration
    • Olivier BJ, Sorensen CM (1990) Variable aggregation rates in colloidal gold: kernel homogeneity dependence on aggregant concentration. Phys Rev A 41:2093-2100.
    • (1990) Phys Rev A , vol.41 , pp. 2093-2100
    • Olivier, B.J.1    Sorensen, C.M.2
  • 46
    • 0034650756 scopus 로고    scopus 로고
    • Approximate population balance equations for aggregation-breakage processes
    • Vanni M (2000) Approximate population balance equations for aggregation-breakage processes. J Colloid Interface Sci 221:143-160.
    • (2000) J Colloid Interface Sci , vol.221 , pp. 143-160
    • Vanni, M.1
  • 47
    • 0032940179 scopus 로고    scopus 로고
    • Kinetic study on thermal denaturation of hen egg-white lysozyme involving precipitation
    • Nohara D, Mizutani A, Sakai T (1999) Kinetic study on thermal denaturation of hen egg-white lysozyme involving precipitation. J Biosci Bioeng 87:199-205.
    • (1999) J Biosci Bioeng , vol.87 , pp. 199-205
    • Nohara, D.1    Mizutani, A.2    Sakai, T.3
  • 48
    • 28844482969 scopus 로고    scopus 로고
    • The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways
    • Librizzi F, Rischel C (2005) The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways. Protein Sci 14:3129-3134.
    • (2005) Protein Sci , vol.14 , pp. 3129-3134
    • Librizzi, F.1    Rischel, C.2
  • 50
    • 33745413982 scopus 로고    scopus 로고
    • Protein structural conformation and not second virial coefficient relates to long-term irreversible aggregation of a monoclonal antibody and oval-bumin in solution
    • Bajaj H, Sharma VK, Badkar A, Zeng D, Nema S, Kalonia DS (2006) Protein structural conformation and not second virial coefficient relates to long-term irreversible aggregation of a monoclonal antibody and oval-bumin in solution. Pharm Res 23:1382-1394.
    • (2006) Pharm Res , vol.23 , pp. 1382-1394
    • Bajaj, H.1    Sharma, V.K.2    Badkar, A.3    Zeng, D.4    Nema, S.5    Kalonia, D.S.6
  • 51
    • 0034237295 scopus 로고    scopus 로고
    • Lower kinetic limit to protein thermal stability: A proposal regarding protein stability in vivo and its relation with misfolding diseases
    • Plaza del Pino IM, Ibarra-Molero B, Sánchez-Ruiz JM (2000) Lower kinetic limit to protein thermal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases. Proteins 40:58-70.
    • (2000) Proteins , vol.40 , pp. 58-70
    • Plaza del Pino, I.M.1    Ibarra-Molero, B.2    Sánchez-Ruiz, J.M.3
  • 52
    • 0038161224 scopus 로고    scopus 로고
    • Revisiting the method of cumulants for the analysis of dynamic light-scattering data
    • Frisken BJ (2001) Revisiting the method of cumulants for the analysis of dynamic light-scattering data. Appl Opt 40:4087-4091.
    • (2001) Appl Opt , vol.40 , pp. 4087-4091
    • Frisken, B.J.1
  • 53
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • García de la Torre J, Huertas ML, Carrasco B (2000) Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys J 78: 719-730.
    • (2000) Biophys J , vol.78 , pp. 719-730
    • García de la Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 56
    • 44649133131 scopus 로고    scopus 로고
    • Extrinsic fluorescent dyes as tools for protein characterization
    • Hawe A, Sutter M, Jiskoot W (2008) Extrinsic fluorescent dyes as tools for protein characterization. Pharm Res 25:1487-1499.
    • (2008) Pharm Res , vol.25 , pp. 1487-1499
    • Hawe, A.1    Sutter, M.2    Jiskoot, W.3


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