메뉴 건너뛰기




Volumn 908, Issue , 2016, Pages 168-176

Characterization of cetuximab Fc/2 dimers by off-line CZE-MS

Author keywords

Capillary electrophoresis mass spectrometry; Dimers; Monoclonal antibody; NanoElectrospray

Indexed keywords

AMINO ACIDS; CAPILLARY ELECTROPHORESIS; CHARACTERIZATION; DIMERS; ELECTROPHORESIS; GLYCOSYLATION; MASS SPECTROMETRY; MONOCLONAL ANTIBODIES; PROTEINS; SEPARATION; SPECTROMETRY;

EID: 84955686112     PISSN: 00032670     EISSN: 18734324     Source Type: Journal    
DOI: 10.1016/j.aca.2015.12.033     Document Type: Article
Times cited : (47)

References (35)
  • 1
    • 77951586447 scopus 로고    scopus 로고
    • Strategies and challenges for the next generation of therapeutic antibodies
    • Beck A., Wurch T., Bailly C., Corvaia N. Strategies and challenges for the next generation of therapeutic antibodies. Nat. Rev. Immunol. 2010, 10:345-352.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 345-352
    • Beck, A.1    Wurch, T.2    Bailly, C.3    Corvaia, N.4
  • 2
    • 84860896956 scopus 로고    scopus 로고
    • Marketed therapeutic antibodies compendium
    • Reichert J.M. Marketed therapeutic antibodies compendium. mAbs 2012, 4:413-415.
    • (2012) mAbs , vol.4 , pp. 413-415
    • Reichert, J.M.1
  • 4
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold J.N., Wormald M.R., Sim R.B., Rudd P.M., Dwek R.A. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 2007, 25:21-50.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 5
    • 59149092065 scopus 로고    scopus 로고
    • Mass spectrometry for structural characteization of therapeutic antibodies
    • Zhang Z.Q., Pan H., Chen X.Y. Mass spectrometry for structural characteization of therapeutic antibodies. Mass Spectrom. Rev. 2009, 28:147-176.
    • (2009) Mass Spectrom. Rev. , vol.28 , pp. 147-176
    • Zhang, Z.Q.1    Pan, H.2    Chen, X.Y.3
  • 7
    • 38749103119 scopus 로고    scopus 로고
    • The immunoglobulin constant region contributes to affinity and specificity
    • Torres M., Casadevall A. The immunoglobulin constant region contributes to affinity and specificity. Trends Immunol. 2008, 29:91-97.
    • (2008) Trends Immunol. , vol.29 , pp. 91-97
    • Torres, M.1    Casadevall, A.2
  • 8
    • 0030856842 scopus 로고    scopus 로고
    • Protein aggregates seem to play a key role among the parameters influencing the antigenicity of interferon alpha (IFN-α) in normal and transgenic mice
    • Braun A., Kwee L., Labow M., Alsenz J. Protein aggregates seem to play a key role among the parameters influencing the antigenicity of interferon alpha (IFN-α) in normal and transgenic mice. Pharm. Res. 1997, 14:1472-1478.
    • (1997) Pharm. Res. , vol.14 , pp. 1472-1478
    • Braun, A.1    Kwee, L.2    Labow, M.3    Alsenz, J.4
  • 9
    • 0036598634 scopus 로고    scopus 로고
    • Bioequivalence and the immunogenicity of biopharmaceuticals
    • Schellekens H. Bioequivalence and the immunogenicity of biopharmaceuticals. Nat. Rev. Drug. Discov. 2002, 1:457-462.
    • (2002) Nat. Rev. Drug. Discov. , vol.1 , pp. 457-462
    • Schellekens, H.1
  • 11
    • 76749130326 scopus 로고    scopus 로고
    • Aggregation of a multidomain protein: a coagulation mechanism governs aggregation of a model IgG1 antibody under weak thermal stress
    • Andersen C.B., Manno M., Rischel C., Thorolfsson M., Martorana V. Aggregation of a multidomain protein: a coagulation mechanism governs aggregation of a model IgG1 antibody under weak thermal stress. Prot. Sci. 2010, 19:279-290.
    • (2010) Prot. Sci. , vol.19 , pp. 279-290
    • Andersen, C.B.1    Manno, M.2    Rischel, C.3    Thorolfsson, M.4    Martorana, V.5
  • 12
    • 79954531753 scopus 로고    scopus 로고
    • Nonnative aggregation of an IgG1 antibody in acidic conditions: part 1. unfolding, colloidal interactions, and formation of high-molecular-weight aggregates
    • Brummitt R.K., Nesta D.P., Chang L.Q., Chase S.F., Laue T.M., Roberts C.J. Nonnative aggregation of an IgG1 antibody in acidic conditions: part 1. unfolding, colloidal interactions, and formation of high-molecular-weight aggregates. J. Pharm. Sci. 2011, 100:2087-2103.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2087-2103
    • Brummitt, R.K.1    Nesta, D.P.2    Chang, L.Q.3    Chase, S.F.4    Laue, T.M.5    Roberts, C.J.6
  • 13
    • 84861842454 scopus 로고    scopus 로고
    • Biosimilar, biobetter, and next generation antibody characterization by mass spectrometry
    • Beck A., Sanglier-Cianferani S., Van Dorsselaer A. Biosimilar, biobetter, and next generation antibody characterization by mass spectrometry. Anal. Chem. 2012, 84:4637-4646.
    • (2012) Anal. Chem. , vol.84 , pp. 4637-4646
    • Beck, A.1    Sanglier-Cianferani, S.2    Van Dorsselaer, A.3
  • 16
    • 84920847485 scopus 로고    scopus 로고
    • Monoclonal antibodies biosimilarity assessment using transient isotachophoresis capillary zone electrophoresis-tandem mass spectrometry
    • Gahoual R., Biacchi M., Chicher J., Kuhn L., Hammann P., Beck A., Leize-Wagner E., Francois Y.N. Monoclonal antibodies biosimilarity assessment using transient isotachophoresis capillary zone electrophoresis-tandem mass spectrometry. Mabs 2014, 6:1464-1473.
    • (2014) Mabs , vol.6 , pp. 1464-1473
    • Gahoual, R.1    Biacchi, M.2    Chicher, J.3    Kuhn, L.4    Hammann, P.5    Beck, A.6    Leize-Wagner, E.7    Francois, Y.N.8
  • 17
    • 84912144040 scopus 로고    scopus 로고
    • Full antibody primary structure and microvariant characterization in a single injection using transient isotachophoresis and sheathless capillary electrophoresis-tandem mass spectrometry
    • Gahoual R., Busnel J.-M., Beck A., François Y.-N., Leize-Wagner E. Full antibody primary structure and microvariant characterization in a single injection using transient isotachophoresis and sheathless capillary electrophoresis-tandem mass spectrometry. Anal. Chem. 2014, 86:9074-9081.
    • (2014) Anal. Chem. , vol.86 , pp. 9074-9081
    • Gahoual, R.1    Busnel, J.-M.2    Beck, A.3    François, Y.-N.4    Leize-Wagner, E.5
  • 18
    • 84922511434 scopus 로고    scopus 로고
    • Sheathless capillary electrophoresis-tandem mass spectrometry for top-down characterization of Pyrococcus furiosus proteins on a proteome scale
    • Han X., Wang Y., Aslanian A., Bern M., Lavallee-Adam M., Yates J.R. Sheathless capillary electrophoresis-tandem mass spectrometry for top-down characterization of Pyrococcus furiosus proteins on a proteome scale. Anal. Chem. 2014, 86:11006-11012.
    • (2014) Anal. Chem. , vol.86 , pp. 11006-11012
    • Han, X.1    Wang, Y.2    Aslanian, A.3    Bern, M.4    Lavallee-Adam, M.5    Yates, J.R.6
  • 19
    • 84879241038 scopus 로고    scopus 로고
    • Fast top-down intact protein characterization with capillary zone electrophoresis-electrospray ionization tandem mass spectrometry
    • Sun L.L., Knierman M.D., Zhu G.J., Dovichi N.J. Fast top-down intact protein characterization with capillary zone electrophoresis-electrospray ionization tandem mass spectrometry. Anal. Chem. 2013, 85:5989-5995.
    • (2013) Anal. Chem. , vol.85 , pp. 5989-5995
    • Sun, L.L.1    Knierman, M.D.2    Zhu, G.J.3    Dovichi, N.J.4
  • 22
    • 84923196866 scopus 로고    scopus 로고
    • Integrated microfluidic capillary electrophoresis-electrospray ionization devices with online MS detection for the separation and characterization of intact monoclonal antibody variants
    • Redman E.A., Batz N.G., Mellors J.S., Ramsey J.M. Integrated microfluidic capillary electrophoresis-electrospray ionization devices with online MS detection for the separation and characterization of intact monoclonal antibody variants. Anal. Chem. 2015, 87:2264-2272.
    • (2015) Anal. Chem. , vol.87 , pp. 2264-2272
    • Redman, E.A.1    Batz, N.G.2    Mellors, J.S.3    Ramsey, J.M.4
  • 23
    • 84934918462 scopus 로고    scopus 로고
    • Glycoform separation and characterization of cetuximab variants by middle-up off-line capillary zone electrophoresis-UV/electrospray ionization-MS
    • Biacchi M., Gahoual R., Said N., Beck A., Leize-Wagner E., François Y.-N. Glycoform separation and characterization of cetuximab variants by middle-up off-line capillary zone electrophoresis-UV/electrospray ionization-MS. Anal. Chem. 2015, 87:6240-6250.
    • (2015) Anal. Chem. , vol.87 , pp. 6240-6250
    • Biacchi, M.1    Gahoual, R.2    Said, N.3    Beck, A.4    Leize-Wagner, E.5    François, Y.-N.6
  • 25
    • 10644276295 scopus 로고    scopus 로고
    • Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite binding
    • Vincents B., von Pawel-Rammingen U., Bjorck L., Abrahamson M. Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite binding. Biochem. 2004, 43:15540-15549.
    • (2004) Biochem. , vol.43 , pp. 15540-15549
    • Vincents, B.1    von Pawel-Rammingen, U.2    Bjorck, L.3    Abrahamson, M.4
  • 26
    • 84883860531 scopus 로고    scopus 로고
    • Correct primary structure assessment and extensive glyco-profiling of cetuximab by a combination of intact, middle-up, middle-down and bottom-up ESI and MALDI mass spectrometry techniques
    • Ayoub D., Jabs W., Resemann A., Evers W., Evans C., Main L., Baessmann C., Wagner-Rousset E., Suckau D., Beck A. Correct primary structure assessment and extensive glyco-profiling of cetuximab by a combination of intact, middle-up, middle-down and bottom-up ESI and MALDI mass spectrometry techniques. Mabs 2013, 5:699-710.
    • (2013) Mabs , vol.5 , pp. 699-710
    • Ayoub, D.1    Jabs, W.2    Resemann, A.3    Evers, W.4    Evans, C.5    Main, L.6    Baessmann, C.7    Wagner-Rousset, E.8    Suckau, D.9    Beck, A.10
  • 27
    • 84954233082 scopus 로고    scopus 로고
    • Weak protein interactions and pH- and temperature-dependent aggregation of human Fc1
    • Wu H., Truncali K., Ritchie J., Kroe-Barrett R., Singh S., Robinson A.S., Roberts C.J. Weak protein interactions and pH- and temperature-dependent aggregation of human Fc1. mAbs 2015, 7(6):1072-1083.
    • (2015) mAbs , vol.7 , Issue.6 , pp. 1072-1083
    • Wu, H.1    Truncali, K.2    Ritchie, J.3    Kroe-Barrett, R.4    Singh, S.5    Robinson, A.S.6    Roberts, C.J.7
  • 28
    • 0001733106 scopus 로고    scopus 로고
    • High-resolution capillary isoelectric focusing of proteins using highly hydrophilic-substituted cellulose-coated capillaries
    • Shen Y.F., Smith R.D. High-resolution capillary isoelectric focusing of proteins using highly hydrophilic-substituted cellulose-coated capillaries. J. Microcolumn Sep. 2000, 12:135-141.
    • (2000) J. Microcolumn Sep. , vol.12 , pp. 135-141
    • Shen, Y.F.1    Smith, R.D.2
  • 30
    • 31744447070 scopus 로고    scopus 로고
    • Glycosylation in the Fc domain of IgG increases resistance to proteolytic cleavage by papain
    • Raju T.S., Scallon B.J. Glycosylation in the Fc domain of IgG increases resistance to proteolytic cleavage by papain. Biochem. Biophys. Res. Co. 2006, 341:797-803.
    • (2006) Biochem. Biophys. Res. Co. , vol.341 , pp. 797-803
    • Raju, T.S.1    Scallon, B.J.2
  • 31
    • 34249707388 scopus 로고    scopus 로고
    • Analysis of lysine clipping of a humanized Lewis-Y specific IgG antibody and its relation to Fc-mediated effector function
    • Antes B., Amon S., Rizzi A., Wiederkum S., Kainer M., Szolar O., Fido M., Kircheis R., Nechansky A. Analysis of lysine clipping of a humanized Lewis-Y specific IgG antibody and its relation to Fc-mediated effector function. J. Chromatogr. B 2007, 852:250-256.
    • (2007) J. Chromatogr. B , vol.852 , pp. 250-256
    • Antes, B.1    Amon, S.2    Rizzi, A.3    Wiederkum, S.4    Kainer, M.5    Szolar, O.6    Fido, M.7    Kircheis, R.8    Nechansky, A.9
  • 32
    • 84894903134 scopus 로고    scopus 로고
    • Novel sheathless CE-MS interface as an original and powerful infusion platform for nanoESI study: from intact proteins to high molecular mass noncovalent complexes
    • Gahoual R., Busnel J.M., Wolff P., Francois Y.N., Leize-Wagner E. Novel sheathless CE-MS interface as an original and powerful infusion platform for nanoESI study: from intact proteins to high molecular mass noncovalent complexes. Anal. Bioanal. Chem. 2014, 406:1029-1038.
    • (2014) Anal. Bioanal. Chem. , vol.406 , pp. 1029-1038
    • Gahoual, R.1    Busnel, J.M.2    Wolff, P.3    Francois, Y.N.4    Leize-Wagner, E.5
  • 33
    • 0032555738 scopus 로고    scopus 로고
    • Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry
    • Nettleton E.J., Sunde M., Lai Z.H., Kelly J.W., Dobson C.M., Robinson C.V. Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry. J. Mol. Biol. 1998, 281:553-564.
    • (1998) J. Mol. Biol. , vol.281 , pp. 553-564
    • Nettleton, E.J.1    Sunde, M.2    Lai, Z.H.3    Kelly, J.W.4    Dobson, C.M.5    Robinson, C.V.6
  • 35
    • 58249083162 scopus 로고    scopus 로고
    • How to deal with weak interactions in noncovalent complexes analyzed by electrospray mass spectrometry: cyclopeptidic inhibitors of the nuclear receptor coactivator 1-STAT6
    • Touboul D., Maillard L., Grasslin A., Moumne R., Seitz M., Robinson J., Zenobi R. How to deal with weak interactions in noncovalent complexes analyzed by electrospray mass spectrometry: cyclopeptidic inhibitors of the nuclear receptor coactivator 1-STAT6. J. Am. Soc. Mass Spectrom. 2009, 20:303-311.
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 303-311
    • Touboul, D.1    Maillard, L.2    Grasslin, A.3    Moumne, R.4    Seitz, M.5    Robinson, J.6    Zenobi, R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.