메뉴 건너뛰기




Volumn 100, Issue 6, 2011, Pages 2120-2135

High throughput formulation screening for global aggregation behaviors of three monoclonal antibodies

Author keywords

Fluorescence spectroscopy; High throughput technologies; Light scattering; Monoclonal antibody; Protein aggregation; Protein formulation; Stability

Indexed keywords

IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G2; MONOCLONAL ANTIBODY;

EID: 79954498279     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.22450     Document Type: Article
Times cited : (53)

References (40)
  • 1
    • 33845923234 scopus 로고    scopus 로고
    • High throughput screening of protein formulation stability: Practical considerations
    • Capelle MA, Gurny R, Arvinte T. 2007. High throughput screening of protein formulation stability: Practical considerations. Eur J Pharm Biopharm 65(2):131-148.
    • (2007) Eur J Pharm Biopharm , vol.65 , Issue.2 , pp. 131-148
    • Capelle, M.A.1    Gurny, R.2    Arvinte, T.3
  • 2
    • 60649093306 scopus 로고    scopus 로고
    • High throughput methods of assessing protein stability and aggregation
    • Senisterra GA, Finerty PJ Jr. 2009. High throughput methods of assessing protein stability and aggregation. Mol Biosyst 5(3):217-223.
    • (2009) Mol Biosyst , vol.5 , Issue.3 , pp. 217-223
    • Senisterra, G.A.1    Finerty Jr., P.J.2
  • 3
    • 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(9):1325-1336.
    • (2003) Pharm Res , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 4
    • 84919873764 scopus 로고    scopus 로고
    • Non-native protein aggregation: Pathways, kinetics, and shelf-life prediction
    • In ; Murphy RM, Tsai AM, Eds. New York: Springer
    • Roberts CJ. 2006. Non-native protein aggregation: Pathways, kinetics, and shelf-life prediction. In Misbehaving proteins: Protein misfolding, aggregation, and stability; Murphy RM, Tsai AM, Eds. New York: Springer, pp 17-46.
    • (2006) Misbehaving proteins: Protein misfolding, aggregation, and stability , pp. 17-46
    • Roberts, C.J.1
  • 5
    • 67449132077 scopus 로고    scopus 로고
    • Principles, approaches, and challenges for predicting protein aggregation rates and shelf life
    • Weiss WF IV, Young TM, Roberts CJ. 2009. Principles, approaches, and challenges for predicting protein aggregation rates and shelf life. J Pharm Sci 98(4):1246-1277.
    • (2009) J Pharm Sci , vol.98 , Issue.4 , pp. 1246-1277
    • Weiss, W.I.1    Young, T.M.2    Roberts, C.J.3
  • 6
    • 0024694268 scopus 로고
    • Practical considerations in the production, purification, and formulation of monoclonal antibodies for immunoscintigraphy and immunotherapy
    • Bogard WC Jr, Dean RT, Deo Y, Fuchs R, Mattis JA, McLean AA, Berger HJ. 1989. Practical considerations in the production, purification, and formulation of monoclonal antibodies for immunoscintigraphy and immunotherapy. Semin Nucl Med 19(3):202-220.
    • (1989) Semin Nucl Med , vol.19 , Issue.3 , pp. 202-220
    • Bogard Jr, W.C.1    Dean, R.T.2    Deo, Y.3    Fuchs, R.4    Mattis, J.A.5    McLean, A.A.6    Berger, H.J.7
  • 7
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • Shire SJ, Shahrokh Z, Liu J. 2004. Challenges in the development of high protein concentration formulations. J Pharm Sci 93(6):1390-1402.
    • (2004) J Pharm Sci , vol.93 , Issue.6 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 8
    • 33846140780 scopus 로고    scopus 로고
    • Antibody structure, instability, and formulation
    • Wang W, Singh S, Zeng DL, King K, Nema S. 2007. Antibody structure, instability, and formulation. J Pharm Sci 96(1):1-26.
    • (2007) J Pharm Sci , vol.96 , Issue.1 , pp. 1-26
    • Wang, W.1    Singh, S.2    Zeng, D.L.3    King, K.4    Nema, S.5
  • 9
    • 33747488943 scopus 로고    scopus 로고
    • Formulation and delivery issues for monoclonal antibody therapeutics
    • Daugherty AL, Mrsny RJ. 2006. Formulation and delivery issues for monoclonal antibody therapeutics. Adv Drug Deliv Rev 58(5-6):686-706.
    • (2006) Adv Drug Deliv Rev , vol.58 , Issue.5-6 , pp. 686-706
    • Daugherty, A.L.1    Mrsny, R.J.2
  • 10
    • 69249215475 scopus 로고    scopus 로고
    • A critical review of analytical methods for subvisible and visible particles
    • Narhi LO, Jiang Y, Cao S, Benedek K, Shnek D. 2009. A critical review of analytical methods for subvisible and visible particles. Curr Pharm Biotechnol 10(4):373-381.
    • (2009) Curr Pharm Biotechnol , vol.10 , Issue.4 , pp. 373-381
    • Narhi, L.O.1    Jiang, Y.2    Cao, S.3    Benedek, K.4    Shnek, D.5
  • 12
    • 67650072650 scopus 로고    scopus 로고
    • Lumry-Eyring nucleated-polymerization model of protein aggregation kinetics. 2. Competing growth via condensation and chain polymerization
    • Li Y, Roberts CJ. 2009. Lumry-Eyring nucleated-polymerization model of protein aggregation kinetics. 2. Competing growth via condensation and chain polymerization. J Phys Chem B 113(19):7020-7032.
    • (2009) J Phys Chem B , vol.113 , Issue.19 , pp. 7020-7032
    • Li, Y.1    Roberts, C.J.2
  • 14
    • 42749089622 scopus 로고    scopus 로고
    • High throughput quantification of mutant huntingtin aggregates
    • Scotter EL, Narayan P, Glass M, Dragunow M. 2008. High throughput quantification of mutant huntingtin aggregates. J Neurosci Methods 171(1):174-179.
    • (2008) J Neurosci Methods , vol.171 , Issue.1 , pp. 174-179
    • Scotter, E.L.1    Narayan, P.2    Glass, M.3    Dragunow, M.4
  • 15
    • 68849119871 scopus 로고    scopus 로고
    • High-throughput screening of optimal solution conditions for structural biological studies by fluorescence correlation spectroscopy
    • Sugiki T, Yoshiura C, Kofuku Y, Ueda T, Shimada I, Takahashi H. 2009. High-throughput screening of optimal solution conditions for structural biological studies by fluorescence correlation spectroscopy. Protein Sci 18(5):1115-1120.
    • (2009) Protein Sci , vol.18 , Issue.5 , pp. 1115-1120
    • Sugiki, T.1    Yoshiura, C.2    Kofuku, Y.3    Ueda, T.4    Shimada, I.5    Takahashi, H.6
  • 16
    • 33750449952 scopus 로고    scopus 로고
    • A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide
    • Kim W, Kim Y, Min J, Kim DJ, Chang YT, Hecht MH. 2006. A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide. ACS Chem Biol 1(7):461-469.
    • (2006) ACS Chem Biol , vol.1 , Issue.7 , pp. 461-469
    • Kim, W.1    Kim, Y.2    Min, J.3    Kim, D.J.4    Chang, Y.T.5    Hecht, M.H.6
  • 17
    • 64849106509 scopus 로고    scopus 로고
    • High-throughput analysis of Alzheimer's beta-amyloid aggregation using a microfluidic self-assembly of monomers
    • Lee JS, Ryu J, Park CB. 2009. High-throughput analysis of Alzheimer's beta-amyloid aggregation using a microfluidic self-assembly of monomers. Anal Chem 81(7):2751-2759.
    • (2009) Anal Chem , vol.81 , Issue.7 , pp. 2751-2759
    • Lee, J.S.1    Ryu, J.2    Park, C.B.3
  • 18
    • 77949789023 scopus 로고    scopus 로고
    • High throughput thermostability screening of monoclonal antibody formulations
    • He F, Hogan S, Latypov RF, Narhi LO, Razinkov VI. 2010. High throughput thermostability screening of monoclonal antibody formulations. J Pharm Sci 99(4):1707-1720.
    • (2010) J Pharm Sci , vol.99 , Issue.4 , pp. 1707-1720
    • He, F.1    Hogan, S.2    Latypov, R.F.3    Narhi, L.O.4    Razinkov, V.I.5
  • 19
    • 74049123780 scopus 로고    scopus 로고
    • Multi-variate approach to global protein aggregation behavior and kinetics: effects of pH, NaCl, and temperature for alpha-chymotrypsinogen A
    • Li Y, Ogunnaike BA, Roberts CJ. 2010. Multi-variate approach to global protein aggregation behavior and kinetics: effects of pH, NaCl, and temperature for alpha-chymotrypsinogen A. J Pharm Sci 99(2):645-662.
    • (2010) J Pharm Sci , vol.99 , Issue.2 , pp. 645-662
    • Li, Y.1    Ogunnaike, B.A.2    Roberts, C.J.3
  • 20
    • 78049249356 scopus 로고    scopus 로고
    • Comparative effects of pH and ionic strength on protein-protein interactions, unfolding, and aggregation for IgG1 antibodies
    • 99(12):4830-4848.
    • Sahin E, Grillo AO, Perkins MD, Roberts CJ. Comparative effects of pH and ionic strength on protein-protein interactions, unfolding, and aggregation for IgG1 antibodies. J Pharm Sci. 99(12):4830-4848.
    • J Pharm Sci.
    • Sahin, E.1    Grillo, A.O.2    Perkins, M.D.3    Roberts, C.J.4
  • 21
    • 34250834054 scopus 로고    scopus 로고
    • A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding
    • Andrews JM, Roberts CJ. 2007. A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding. J Phys Chem B 111(27):7897-7913.
    • (2007) J Phys Chem B , vol.111 , Issue.27 , pp. 7897-7913
    • Andrews, J.M.1    Roberts, C.J.2
  • 22
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state
    • Pallitto MM, Murphy RM. 2001. A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state. Biophys J 81(3):1805-1822.
    • (2001) Biophys J , vol.81 , Issue.3 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 23
    • 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(11):3997-4016
    • (2009) J Pharm Sci.98(11):3997-4016
    • Li, Y.1    Weiss, W.I.2    Roberts, C.J.3
  • 24
    • 85031254225 scopus 로고    scopus 로고
    • Global non-native aggregation behavior for alpha-chymotrypsinogen A. Ph.D. Thesis. Delaware: Department of Chemical Engineering, University of Delaware
    • Li Y. 2009. Global non-native aggregation behavior for alpha-chymotrypsinogen A. Ph.D. Thesis. Delaware: Department of Chemical Engineering, University of Delaware, pp 271.
    • (2009) , pp. 271
    • Li, Y.1
  • 25
    • 0034967751 scopus 로고    scopus 로고
    • Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation
    • Carrotta R, Bauer R, Waninge R, Rischel C. 2001. Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation. Protein Sci 10(7):1312-1318.
    • (2001) Protein Sci , vol.10 , Issue.7 , pp. 1312-1318
    • Carrotta, R.1    Bauer, R.2    Waninge, R.3    Rischel, C.4
  • 27
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink AL. 1998. Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Fold Des 3(1):R9-R23.
    • (1998) Fold Des , vol.3 , Issue.1
    • Fink, A.L.1
  • 28
    • 68949085124 scopus 로고    scopus 로고
    • Protein aggregation: Pathways, induction factors and analysis
    • Mahler HC, Friess W, Grauschopf U, Kiese S. 2008. Protein aggregation: Pathways, induction factors and analysis. J Pharm Sci. 98(9):2909-2934.
    • (2008) J Pharm Sci. , vol.98 , Issue.9 , pp. 2909-2934
    • Mahler, H.C.1    Friess, W.2    Grauschopf, U.3    Kiese, S.4
  • 29
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • Roberts CJ. 2007. Non-native protein aggregation kinetics. Biotechnol Bioeng 98(5):927-938.
    • (2007) Biotechnol Bioeng , vol.98 , Issue.5 , pp. 927-938
    • Roberts, C.J.1
  • 30
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM. 2003. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424(6950):805-808.
    • (2003) Nature , vol.424 , Issue.6950 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 31
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen FH, Berglund H, Vedadi M. 2007. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat Protoc 2(9):2212-2221.
    • (2007) Nat Protoc , vol.2 , Issue.9 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 32
    • 33845567410 scopus 로고    scopus 로고
    • Detection and characterization of protein aggregates by fluorescence microscopy
    • Demeule B, Gurny R, Arvinte T. 2007. Detection and characterization of protein aggregates by fluorescence microscopy. Int J Pharm 329(1-2):37-45.
    • (2007) Int J Pharm , vol.329 , Issue.1-2 , pp. 37-45
    • Demeule, B.1    Gurny, R.2    Arvinte, T.3
  • 33
    • 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(7):1487-1499.
    • (2008) Pharm Res , vol.25 , Issue.7 , pp. 1487-1499
    • Hawe, A.1    Sutter, M.2    Jiskoot, W.3
  • 34
    • 34547174917 scopus 로고    scopus 로고
    • Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins
    • Munishkina LA, Fink AL. 2007. Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins. Biochim Biophys Acta 1768(8):1862-1885.
    • (2007) Biochim Biophys Acta , vol.1768 , Issue.8 , pp. 1862-1885
    • Munishkina, L.A.1    Fink, A.L.2
  • 35
    • 34250870678 scopus 로고    scopus 로고
    • Non-native aggregation of alpha-chymotrypsinogen occurs through nucleation and growth with competing nucleus sizes and negative activation energies
    • Andrews JM, Roberts CJ. 2007. Non-native aggregation of alpha-chymotrypsinogen occurs through nucleation and growth with competing nucleus sizes and negative activation energies. Biochemistry 46(25):7558-7571.
    • (2007) Biochemistry , vol.46 , Issue.25 , pp. 7558-7571
    • Andrews, J.M.1    Roberts, C.J.2
  • 36
    • 0031570763 scopus 로고    scopus 로고
    • Stopped-flow kinetics reveal multiple phases of thioflavin T binding to Alzheimer beta (1-40) amyloid fibrils
    • LeVine H 3rd. 1997. Stopped-flow kinetics reveal multiple phases of thioflavin T binding to Alzheimer beta (1-40) amyloid fibrils. Arch Biochem Biophys 342(2):306-316.
    • (1997) Arch Biochem Biophys , vol.342 , Issue.2 , pp. 306-316
    • LeVine, H.3.1
  • 37
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • Nielsen L, Khurana R, Coats A, Frokjaer S, Brange J, Vyas S, Uversky VN, Fink AL. 2001. Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism. Biochemistry 40(20):6036-6046.
    • (2001) Biochemistry , vol.40 , Issue.20 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 38
    • 22244456042 scopus 로고    scopus 로고
    • Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy
    • Lindgren M, Sorgjerd K, Hammarstrom P. 2005. Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy. Biophys J 88(6):4200-4212.
    • (2005) Biophys J , vol.88 , Issue.6 , pp. 4200-4212
    • Lindgren, M.1    Sorgjerd, K.2    Hammarstrom, P.3
  • 40
    • 68949119488 scopus 로고    scopus 로고
    • Monoclonal antibody interactions with micro- and nanoparticles: Adsorption, aggregation, and accelerated stress studies
    • Bee JS, Chiu D, Sawicki S, Stevenson JL, Chatterjee K, Freund E, Carpenter JF, Randolph TW. 2009. Monoclonal antibody interactions with micro- and nanoparticles: Adsorption, aggregation, and accelerated stress studies. J Pharm Sci 98(9):3218-3238.
    • (2009) J Pharm Sci , vol.98 , Issue.9 , pp. 3218-3238
    • Bee, J.S.1    Chiu, D.2    Sawicki, S.3    Stevenson, J.L.4    Chatterjee, K.5    Freund, E.6    Carpenter, J.F.7    Randolph, T.W.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.