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Volumn 8, Issue 6, 2016, Pages 1021-1034

Advanced assessment of the physicochemical characteristics of Remicade® and Inflectra® by sensitive LC/MS techniques

Author keywords

2D LC; HDMSE; higher order structure; Host cell proteins; hydrogen deuterium exchange; ion mobility spectrometry; N linked glycans; QTof; RapiFluor MS; UPLC

Indexed keywords

GLYCAN; INFLIXIMAB; N GLYCOLOYLNEURAMINIC ACID; BIOSIMILAR AGENT; N-GLYCOLYLNEURAMINIC ACID; NEURAMINIC ACID DERIVATIVE; POLYSACCHARIDE;

EID: 84976600735     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.1080/19420862.2016.1193661     Document Type: Article
Times cited : (38)

References (36)
  • 1
    • 84964523414 scopus 로고    scopus 로고
    • Antibodies to watch in 2016
    • 26651519
    • J.M.Reichert. Antibodies to watch in 2016. MAbs 2016; 8:197-204; PMID:26651519; doi 10.1080/19420862.2015.1125583
    • (2016) MAbs , vol.8 , pp. 197-204
    • Reichert, J.M.1
  • 3
    • 79952715351 scopus 로고    scopus 로고
    • Biosimilar, biobetter and next generation therapeutic antibodies
    • 21285536
    • A.Beck. Biosimilar, biobetter and next generation therapeutic antibodies. MAbs 2011; 3:107-10; PMID:21285536; doi 10.4161/mabs.3.2.14785
    • (2011) MAbs , vol.3 , pp. 107-110
    • Beck, A.1
  • 5
    • 84925363068 scopus 로고    scopus 로고
    • Cutting-edge mass spectrometry characterization of originator, biosimilar and biobetter antibodies
    • 25800010
    • A.Beck, F.Debaene, H.Diemer, E.Wagner-Rousset, O.Colas, A.Van Dorsselaer, S.Cianferani. Cutting-edge mass spectrometry characterization of originator, biosimilar and biobetter antibodies. J Mass Spectrom 2015; 50:285-97; PMID:25800010; doi 10.1002/jms.3554
    • (2015) J Mass Spectrom , vol.50 , pp. 285-297
    • Beck, A.1    Debaene, F.2    Diemer, H.3    Wagner-Rousset, E.4    Colas, O.5    Van Dorsselaer, A.6    Cianferani, S.7
  • 6
    • 84863470971 scopus 로고    scopus 로고
    • Marketing approval of Mogamulizumab: A triumph for glyco-engineering
    • 22699226
    • A.Beck, J.M.Reichert. Marketing approval of Mogamulizumab: A triumph for glyco-engineering. MAbs 2012; 4:419-25; PMID:22699226; doi 10.4161/mabs.20996
    • (2012) MAbs , vol.4 , pp. 419-425
    • Beck, A.1    Reichert, J.M.2
  • 9
    • 84861842454 scopus 로고    scopus 로고
    • Biosimilar, biobetter, and next generation antibody characterization by mass spectrometry
    • 22510259
    • A.Beck, S.Sanglier-Cianferani, A.Van Dorsselaer. Biosimilar, biobetter, and next generation antibody characterization by mass spectrometry. Anal Chem 2012; 84:4637-46; PMID:22510259; doi 10.1021/ac3002885
    • (2012) Anal Chem , vol.84 , pp. 4637-4646
    • Beck, A.1    Sanglier-Cianferani, S.2    Van Dorsselaer, A.3
  • 13
    • 77958549515 scopus 로고    scopus 로고
    • Rapid comparison of a candidate biosimilar to an innovator monoclonal antibody with advanced liquid chromatography and mass spectrometry technologies
    • 20458189
    • H.Xie, A.Chakraborty, J.Ahn, Y.Q.Yu, D.P.Dakshinamoorthy, M.Gilar, W.Chen, S.J.Skilton, J.R.Mazzeo. Rapid comparison of a candidate biosimilar to an innovator monoclonal antibody with advanced liquid chromatography and mass spectrometry technologies. MAbs 2010; 2:379-94; PMID:20458189; doi 10.4161/mabs.11986
    • (2010) MAbs , vol.2 , pp. 379-394
    • Xie, H.1    Chakraborty, A.2    Ahn, J.3    Yu, Y.Q.4    Dakshinamoorthy, D.P.5    Gilar, M.6    Chen, W.7    Skilton, S.J.8    Mazzeo, J.R.9
  • 14
    • 84883880492 scopus 로고    scopus 로고
    • Approval of the first biosimilar antibodies in Europe: A major landmark for the biopharmaceutical industry
    • 23924791
    • A.Beck, J.M.Reichert. Approval of the first biosimilar antibodies in Europe: A major landmark for the biopharmaceutical industry. MAbs 2013; 5:621-3; PMID:23924791; doi 10.4161/mabs.25864
    • (2013) MAbs , vol.5 , pp. 621-623
    • Beck, A.1    Reichert, J.M.2
  • 15
    • 84946495972 scopus 로고    scopus 로고
    • Biosimilar monoclonal antibodies: The scientific basis for extrapolation
    • 26365396
    • H.Schellekens, E.Lietzan, F.Faccin, J.Venema. Biosimilar monoclonal antibodies: The scientific basis for extrapolation. Expert Opin Biol Ther 2015; 15:1633-46; PMID:26365396; doi 10.1517/14712598.2015.1083552
    • (2015) Expert Opin Biol Ther , vol.15 , pp. 1633-1646
    • Schellekens, H.1    Lietzan, E.2    Faccin, F.3    Venema, J.4
  • 17
    • 84929630799 scopus 로고    scopus 로고
    • Rapid preparation of released N-glycans for HILIC analysis using a labeling reagent that facilitates sensitive fluorescence and ESI-MS detection
    • 25927596
    • M.A.Lauber, Y.Q.Yu, D.W.Brousmiche, Z.Hua, S.M.Koza, P.Magnelli, E.Guthrie, C.H.Taron, K.J.Fountain. Rapid preparation of released N-glycans for HILIC analysis using a labeling reagent that facilitates sensitive fluorescence and ESI-MS detection. Anal Chem 2015; 87:5401-9; PMID:25927596; doi 10.1021/acs.analchem.5b00758
    • (2015) Anal Chem , vol.87 , pp. 5401-5409
    • Lauber, M.A.1    Yu, Y.Q.2    Brousmiche, D.W.3    Hua, Z.4    Koza, S.M.5    Magnelli, P.6    Guthrie, E.7    Taron, C.H.8    Fountain, K.J.9
  • 18
    • 33750835115 scopus 로고    scopus 로고
    • Non-fucosylated therapeutic antibodies as next-generation therapeutic antibodies
    • 17049014
    • M.Satoh, S.Iida, K.Shitara. Non-fucosylated therapeutic antibodies as next-generation therapeutic antibodies. Expert Opin Biol Ther 2006; 6:1161-73; PMID:17049014; doi 10.1517/14712598.6.11.1161
    • (2006) Expert Opin Biol Ther , vol.6 , pp. 1161-1173
    • Satoh, M.1    Iida, S.2    Shitara, K.3
  • 19
    • 79954547968 scopus 로고    scopus 로고
    • The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studies
    • 21491437
    • D.Houde, S.A.Berkowitz, J.R.Engen. The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studies. J Pharm Sci 2011; 100:2071-86; PMID:21491437; doi 10.1002/jps.22432
    • (2011) J Pharm Sci , vol.100 , pp. 2071-2086
    • Houde, D.1    Berkowitz, S.A.2    Engen, J.R.3
  • 20
    • 84960376112 scopus 로고    scopus 로고
    • Comprehensive characterization of relationship between higher-order structure and FcRn Binding affinity of stress-exposed monoclonal antibodies
    • 26694753
    • D.Tsuchida, K.Yamazaki, S.Akashi. Comprehensive characterization of relationship between higher-order structure and FcRn Binding affinity of stress-exposed monoclonal antibodies. Pharm Res 2016; 33:994-1002; PMID:26694753; doi 10.1007/s11095-015-1845-5
    • (2016) Pharm Res , vol.33 , pp. 994-1002
    • Tsuchida, D.1    Yamazaki, K.2    Akashi, S.3
  • 21
    • 64849114588 scopus 로고    scopus 로고
    • Characterization of IgG1 conformation and conformational dynamics by hydrogen/deuterium exchange mass spectrometry
    • 19265386
    • D.Houde, J.Arndt, W.Domeier, S.Berkowitz, J.R.Engen. Characterization of IgG1 conformation and conformational dynamics by hydrogen/deuterium exchange mass spectrometry. Anal Chem 2009; 81:2644-51; PMID:19265386; doi 10.1021/ac802575y
    • (2009) Anal Chem , vol.81 , pp. 2644-2651
    • Houde, D.1    Arndt, J.2    Domeier, W.3    Berkowitz, S.4    Engen, J.R.5
  • 22
    • 84958811707 scopus 로고    scopus 로고
    • Effect of Fc-glycan structure on the conformational stability of IgG revealed by hydrogen/deuterium exchange and limited proteolysis
    • 26812426
    • J.Fang, J.Richardson, Z.Du, Z.Zhang. Effect of Fc-glycan structure on the conformational stability of IgG revealed by hydrogen/deuterium exchange and limited proteolysis. Biochemistry 2016; 55:860-8; PMID:26812426; doi 10.1021/acs.biochem.5b01323
    • (2016) Biochemistry , vol.55 , pp. 860-868
    • Fang, J.1    Richardson, J.2    Du, Z.3    Zhang, Z.4
  • 23
    • 77953671214 scopus 로고    scopus 로고
    • Identification of methionine sulfoxide diastereomers in immunoglobulin gamma antibodies using methionine sulfoxide reductase enzymes
    • 20404551
    • H.K.Khor, M.E.Jacoby, T.C.Squier, G.C.Chu, D.Chelius. Identification of methionine sulfoxide diastereomers in immunoglobulin gamma antibodies using methionine sulfoxide reductase enzymes. MAbs 2010; 2:299-308; PMID:20404551; doi 10.4161/mabs.2.3.11755
    • (2010) MAbs , vol.2 , pp. 299-308
    • Khor, H.K.1    Jacoby, M.E.2    Squier, T.C.3    Chu, G.C.4    Chelius, D.5
  • 24
    • 31644446949 scopus 로고    scopus 로고
    • Absolute quantification of proteins by LCMSE: A virtue of parallel MS acquisition
    • 16219938
    • J.C.Silva, M.V.Gorenstein, G.Z.Li, J.P.Vissers, S.J.Geromanos. Absolute quantification of proteins by LCMSE: A virtue of parallel MS acquisition. Mol Cell Proteomics 2006; 5:144-56; PMID:16219938; doi 10.1074/mcp.M500230-MCP200
    • (2006) Mol Cell Proteomics , vol.5 , pp. 144-156
    • Silva, J.C.1    Gorenstein, M.V.2    Li, G.Z.3    Vissers, J.P.4    Geromanos, S.J.5
  • 26
    • 79955665534 scopus 로고    scopus 로고
    • Engineering the variable region of therapeutic IgG antibodies
    • 21406966
    • T.Igawa, H.Tsunoda, T.Kuramochi, Z.Sampei, S.Ishii, K.Hattori. Engineering the variable region of therapeutic IgG antibodies. MAbs 2011; 3:243-252; PMID:21406966; doi 10.4161/mabs.3.3.15234
    • (2011) MAbs , vol.3 , pp. 243-252
    • Igawa, T.1    Tsunoda, H.2    Kuramochi, T.3    Sampei, Z.4    Ishii, S.5    Hattori, K.6
  • 27
    • 84898035199 scopus 로고    scopus 로고
    • Conformational analysis of processivity clamps in solution demonstrates that tertiary structure does not correlate with protein dynamics
    • 24613485
    • J.Fang, P.Nevin, V.Kairys, C.Venclovas, J.R.Engen, P.J.Beuning. Conformational analysis of processivity clamps in solution demonstrates that tertiary structure does not correlate with protein dynamics. Structure 2014; 22:572-81; PMID:24613485; doi 10.1016/j.str.2014.02.001
    • (2014) Structure , vol.22 , pp. 572-581
    • Fang, J.1    Nevin, P.2    Kairys, V.3    Venclovas, C.4    Engen, J.R.5    Beuning, P.J.6
  • 28
    • 77953655331 scopus 로고    scopus 로고
    • Potential aggregation prone regions in biotherapeutics: A survey of commercial monoclonal antibodies
    • 20065649
    • X.Wang, T.K.Das, S.K.Singh, S.Kumar. Potential aggregation prone regions in biotherapeutics: A survey of commercial monoclonal antibodies. MAbs 2009; 1:254-67; PMID:20065649; doi 10.4161/mabs.1.3.8035
    • (2009) MAbs , vol.1 , pp. 254-267
    • Wang, X.1    Das, T.K.2    Singh, S.K.3    Kumar, S.4
  • 29
    • 84945157050 scopus 로고    scopus 로고
    • Enhanced detection of low-abundance host cell protein impurities in high-purity monoclonal antibodies down to 1 ppm using ion mobility mass spectrometry coupled with multidimensional liquid chromatography
    • 26266576
    • C.E.Doneanu, M.Anderson, B.J.Williams, M.A.Lauber, A.Chakraborty, W.Chen. Enhanced detection of low-abundance host cell protein impurities in high-purity monoclonal antibodies down to 1 ppm using ion mobility mass spectrometry coupled with multidimensional liquid chromatography. Anal Chem 2015; 87:10283-91; PMID:26266576; doi 10.1021/acs.analchem.5b02103
    • (2015) Anal Chem , vol.87 , pp. 10283-10291
    • Doneanu, C.E.1    Anderson, M.2    Williams, B.J.3    Lauber, M.A.4    Chakraborty, A.5    Chen, W.6
  • 30
    • 84895071750 scopus 로고    scopus 로고
    • Drift time-specific collision energies enable deep-coverage data-independent acquisition proteomics
    • 24336358
    • U.Distler, J.Kuharev, P.Navarro, Y.Levin, H.Schild, S.Tenzer. Drift time-specific collision energies enable deep-coverage data-independent acquisition proteomics. Nat Methods 2014; 11:167-70; PMID:24336358; doi 10.1038/nmeth.2767
    • (2014) Nat Methods , vol.11 , pp. 167-170
    • Distler, U.1    Kuharev, J.2    Navarro, P.3    Levin, Y.4    Schild, H.5    Tenzer, S.6
  • 31
    • 84962243105 scopus 로고    scopus 로고
    • Label-free quantification in ion mobility-enhanced data-independent acquisition proteomics
    • 27010757
    • U.Distler, J.Kuharev, P.Navarro, S.Tenzer. Label-free quantification in ion mobility-enhanced data-independent acquisition proteomics. Nat Protoc 2016; 11:795-812; PMID:27010757; doi 10.1038/nprot.2016.042
    • (2016) Nat Protoc , vol.11 , pp. 795-812
    • Distler, U.1    Kuharev, J.2    Navarro, P.3    Tenzer, S.4
  • 33
    • 84865511222 scopus 로고    scopus 로고
    • Pepsin immobilized on high-strength hybrid particles for continuous flow online digestion at 10,000 psi
    • 22856522
    • J.Ahn, M.C.Jung, K.Wyndham, Y.Q.Yu, J.R.Engen. Pepsin immobilized on high-strength hybrid particles for continuous flow online digestion at 10,000 psi. Anal Chem 2012; 84:7256-62; PMID:22856522; doi 10.1021/ac301749h
    • (2012) Anal Chem , vol.84 , pp. 7256-7262
    • Ahn, J.1    Jung, M.C.2    Wyndham, K.3    Yu, Y.Q.4    Engen, J.R.5
  • 34
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • 16208684
    • T.E.Wales, J.R.Engen. Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom Rev 2006; 25:158-70; PMID:16208684; doi 10.1002/mas.20064
    • (2006) Mass Spectrom Rev , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 35
    • 79954631167 scopus 로고    scopus 로고
    • False EX1 signatures caused by sample carryover during HX MS analyses
    • 21643454
    • J.Fang, K.D.Rand, P.J.Beuning, J.R.Engen. False EX1 signatures caused by sample carryover during HX MS analyses. Int J Mass Spectrom 2011; 302:19-25; PMID:21643454; doi 10.1016/j.ijms.2010.06.039
    • (2011) Int J Mass Spectrom , vol.302 , pp. 19-25
    • Fang, J.1    Rand, K.D.2    Beuning, P.J.3    Engen, J.R.4
  • 36
    • 84865583665 scopus 로고    scopus 로고
    • Using ion purity scores for enhancing quantitative accuracy and precision in complex proteomics samples
    • 22811061
    • S.J.Geromanos, C.Hughes, S.Ciavarini, J.P.Vissers, J.I.Langridge. Using ion purity scores for enhancing quantitative accuracy and precision in complex proteomics samples. Anal Bioanal Chem 2012; 404:1127-39; PMID:22811061; doi 10.1007/s00216-012-6197-y
    • (2012) Anal Bioanal Chem , vol.404 , pp. 1127-1139
    • Geromanos, S.J.1    Hughes, C.2    Ciavarini, S.3    Vissers, J.P.4    Langridge, J.I.5


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