메뉴 건너뛰기




Volumn 104, Issue 9, 2015, Pages 2824-2831

Selective Oxidation of Methionine and Tryptophan Residues in a Therapeutic IgG1 Molecule

Author keywords

mass spectrometry; methionine; protein A binding; protein oxidation; therapeutic proteins; tryptophan

Indexed keywords

2,2' AZOBIS(2 AMIDINOPROPANE); HYDROGEN PEROXIDE; IMMUNOGLOBULIN G1; METHIONINE; MONOCLONAL ANTIBODY; PROTEIN A; TERT BUTYL HYDROPEROXIDE; TRYPTOPHAN; DYES, REAGENTS, INDICATORS, MARKERS AND BUFFERS; IMMUNOGLOBULIN G; METAL;

EID: 84939269480     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.24509     Document Type: Article
Times cited : (88)

References (33)
  • 2
    • 0029188498 scopus 로고
    • Conditions promoting metal-catalyzed oxidations during immobilized cu-iminodiacetic acid metal affinity-chromatography
    • Krishnamurthy R, Madurawe RD, Bush KD, Lumpkin JA,. 1995. Conditions promoting metal-catalyzed oxidations during immobilized cu-iminodiacetic acid metal affinity-chromatography. Biotechnol Progr 11 (6): 643-650.
    • (1995) Biotechnol Progr , vol.11 , Issue.6 , pp. 643-650
    • Krishnamurthy, R.1    Madurawe, R.D.2    Bush, K.D.3    Lumpkin, J.A.4
  • 3
    • 52449090177 scopus 로고    scopus 로고
    • Polysorbates 20 and 80 used in the formulation of protein biotherapeutics: Structure and degradation pathways
    • Kerwin BA,. 2008. Polysorbates 20 and 80 used in the formulation of protein biotherapeutics: Structure and degradation pathways. J Pharm Sci 97 (8): 2924-2935.
    • (2008) J Pharm Sci , vol.97 , Issue.8 , pp. 2924-2935
    • Kerwin, B.A.1
  • 4
    • 67649654269 scopus 로고    scopus 로고
    • Protein oxidation during long storage: Identification of the oxidation sites in dihydrofolate reductase from Escherichia coli through LC-MS and fragment studies
    • Takenawa T, Yokota A, Oda M, Takahashi H, Iwakura M,. 2009. Protein oxidation during long storage: Identification of the oxidation sites in dihydrofolate reductase from Escherichia coli through LC-MS and fragment studies. J Biochem 145 (4): 517-523.
    • (2009) J Biochem , vol.145 , Issue.4 , pp. 517-523
    • Takenawa, T.1    Yokota, A.2    Oda, M.3    Takahashi, H.4    Iwakura, M.5
  • 5
    • 84895502551 scopus 로고    scopus 로고
    • Oxidation of therapeutic proteins and peptides: Structural and biological consequences
    • Torosantucci R, Schoneich C, Jiskoot W,. 2014. Oxidation of therapeutic proteins and peptides: Structural and biological consequences. Pharm Res 31 (3): 541-553.
    • (2014) Pharm Res , vol.31 , Issue.3 , pp. 541-553
    • Torosantucci, R.1    Schoneich, C.2    Jiskoot, W.3
  • 6
    • 77953671214 scopus 로고    scopus 로고
    • Identification of methionine sulfoxide diastereomers in immunoglobulin gamma antibodies using methionine sulfoxide reductase enzymes
    • Khor HK, Jacoby ME, Squier TC, Chu GC, Chelius D,. 2010. Identification of methionine sulfoxide diastereomers in immunoglobulin gamma antibodies using methionine sulfoxide reductase enzymes. MAbs 2 (3): 299-308.
    • (2010) MAbs , vol.2 , Issue.3 , pp. 299-308
    • Khor, H.K.1    Jacoby, M.E.2    Squier, T.C.3    Chu, G.C.4    Chelius, D.5
  • 7
    • 45849089529 scopus 로고    scopus 로고
    • Effect of methionine oxidation of a recombinant monoclonal antibody on the binding affinity to protein a and protein G
    • Gaza-Bulseco G, Faldu S, Hurkmans K, Chumsae C, Liu H,. 2008. Effect of methionine oxidation of a recombinant monoclonal antibody on the binding affinity to protein A and protein G. J Chromatogr B Analyt Technol Biomed Life Sci 870 (1): 55-62.
    • (2008) J Chromatogr B Analyt Technol Biomed Life Sci , vol.870 , Issue.1 , pp. 55-62
    • Gaza-Bulseco, G.1    Faldu, S.2    Hurkmans, K.3    Chumsae, C.4    Liu, H.5
  • 8
    • 59949104434 scopus 로고    scopus 로고
    • Methionine oxidation in human IgG2 Fc decreases binding affinities to protein a and FcRn
    • Pan H, Chen K, Chu L, Kinderman F, Apostol I, Huang G,. 2009. Methionine oxidation in human IgG2 Fc decreases binding affinities to protein A and FcRn. Protein Sci 18 (2): 424-433.
    • (2009) Protein Sci , vol.18 , Issue.2 , pp. 424-433
    • Pan, H.1    Chen, K.2    Chu, L.3    Kinderman, F.4    Apostol, I.5    Huang, G.6
  • 12
    • 84866413853 scopus 로고    scopus 로고
    • Analytical protein a chromatography as a quantitative tool for the screening of methionine oxidation in monoclonal antibodies
    • Loew C, Knoblich C, Fichtl J, Alt N, Diepold K, Bulau P, Goldbach P, Adler M, Mahler HC, Grauschopf U,. 2012. Analytical protein a chromatography as a quantitative tool for the screening of methionine oxidation in monoclonal antibodies. J Pharm Sci 101 (11): 4248-4257.
    • (2012) J Pharm Sci , vol.101 , Issue.11 , pp. 4248-4257
    • Loew, C.1    Knoblich, C.2    Fichtl, J.3    Alt, N.4    Diepold, K.5    Bulau, P.6    Goldbach, P.7    Adler, M.8    Mahler, H.C.9    Grauschopf, U.10
  • 14
    • 79952291899 scopus 로고    scopus 로고
    • Identification of potential sites for tryptophan oxidation in recombinant antibodies using tert-butylhydroperoxide and quantitative LC-MS
    • Hensel M, Steurer R, Fichtl J, Elger C, Wedekind F, Petzold A, Schlothauer T, Molhoj M, Reusch D, Bulau P,. 2011. Identification of potential sites for tryptophan oxidation in recombinant antibodies using tert-butylhydroperoxide and quantitative LC-MS. PloS One 6 (3): e17708.
    • (2011) PloS One , vol.6 , Issue.3 , pp. e17708
    • Hensel, M.1    Steurer, R.2    Fichtl, J.3    Elger, C.4    Wedekind, F.5    Petzold, A.6    Schlothauer, T.7    Molhoj, M.8    Reusch, D.9    Bulau, P.10
  • 15
    • 34247125652 scopus 로고    scopus 로고
    • Identification of a single tryptophan residue as critical for binding activity in a humanized monoclonal antibody against respiratory syncytial virus
    • Wei ZP, Feng JH, Lin HY, Mullapudi S, Bishop E, Tous GI, Casas-Finet J, Hakki F, Strouse R, Schenerman MA,. 2007. Identification of a single tryptophan residue as critical for binding activity in a humanized monoclonal antibody against respiratory syncytial virus. Anal Chem 79 (7): 2797-2805.
    • (2007) Anal Chem , vol.79 , Issue.7 , pp. 2797-2805
    • Wei, Z.P.1    Feng, J.H.2    Lin, H.Y.3    Mullapudi, S.4    Bishop, E.5    Tous, G.I.6    Casas-Finet, J.7    Hakki, F.8    Strouse, R.9    Schenerman, M.A.10
  • 18
    • 0029637161 scopus 로고
    • Chemical instability of protein pharmaceuticals: Mechanisms of oxidation and strategies for stabilization
    • Li S, Schoneich C, Borchardt RT,. 1995. Chemical instability of protein pharmaceuticals: Mechanisms of oxidation and strategies for stabilization. Biotechnol Bioeng 48 (5): 490-500.
    • (1995) Biotechnol Bioeng , vol.48 , Issue.5 , pp. 490-500
    • Li, S.1    Schoneich, C.2    Borchardt, R.T.3
  • 19
    • 83555168209 scopus 로고    scopus 로고
    • Reactive impurities in excipients: Profiling, identification and mitigation of drug-excipient incompatibility
    • Wu Y, Levons J, Narang AS, Raghavan K, Rao VM,. 2011. Reactive impurities in excipients: Profiling, identification and mitigation of drug-excipient incompatibility. AAPS PharmSciTech 12 (4): 1248-1263.
    • (2011) AAPS PharmSciTech , vol.12 , Issue.4 , pp. 1248-1263
    • Wu, Y.1    Levons, J.2    Narang, A.S.3    Raghavan, K.4    Rao, V.M.5
  • 20
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization, and formulation of liquid protein pharmaceuticals
    • Wang W,. 1999. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int J Pharm 185 (2): 129-188.
    • (1999) Int J Pharm , vol.185 , Issue.2 , pp. 129-188
    • Wang, W.1
  • 21
    • 84873327051 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation of protein methionine residues in human parathyroid hormone (1-34): Formation of homocysteine and a novel methionine-dependent hydrolysis reaction
    • Mozziconacci O, Ji JA, Wang YJ, Schoneich C,. 2013. Metal-catalyzed oxidation of protein methionine residues in human parathyroid hormone (1-34): Formation of homocysteine and a novel methionine-dependent hydrolysis reaction. Mol Pharm 10 (2): 739-755.
    • (2013) Mol Pharm , vol.10 , Issue.2 , pp. 739-755
    • Mozziconacci, O.1    Ji, J.A.2    Wang, Y.J.3    Schoneich, C.4
  • 22
    • 71649111656 scopus 로고    scopus 로고
    • Methionine, tryptophan, and histidine oxidation in a model protein, PTH: Mechanisms and stabilization
    • Ji JA, Zhang B, Cheng W, Wang YJ,. 2009. Methionine, tryptophan, and histidine oxidation in a model protein, PTH: Mechanisms and stabilization. J Pharm Sci 98 (12): 4485-4500.
    • (2009) J Pharm Sci , vol.98 , Issue.12 , pp. 4485-4500
    • Ji, J.A.1    Zhang, B.2    Cheng, W.3    Wang, Y.J.4
  • 23
    • 0030724407 scopus 로고    scopus 로고
    • Antioxidants for prevention of methionine oxidation in recombinant monoclonal antibody HER2
    • Lam XM, Yang JY, Cleland JL,. 1997. Antioxidants for prevention of methionine oxidation in recombinant monoclonal antibody HER2. J Pharm Sci 86 (11): 1250-1255.
    • (1997) J Pharm Sci , vol.86 , Issue.11 , pp. 1250-1255
    • Lam, X.M.1    Yang, J.Y.2    Cleland, J.L.3
  • 24
    • 0029875931 scopus 로고    scopus 로고
    • The use of t-butyl hydroperoxide as a probe for methionine oxidation in proteins
    • Keck RG,. 1996. The use of t-butyl hydroperoxide as a probe for methionine oxidation in proteins. Anal Biochem 236 (1): 56-62.
    • (1996) Anal Biochem , vol.236 , Issue.1 , pp. 56-62
    • Keck, R.G.1
  • 26
    • 79960135244 scopus 로고    scopus 로고
    • Chemical modifications in therapeutic protein aggregates generated under different stress conditions
    • Luo Q, Joubert MK, Stevenson R, Ketchem RR, Narhi LO, Wypych J,. 2011. Chemical modifications in therapeutic protein aggregates generated under different stress conditions. J Biol Chem 286 (28): 25134-25144.
    • (2011) J Biol Chem , vol.286 , Issue.28 , pp. 25134-25144
    • Luo, Q.1    Joubert, M.K.2    Stevenson, R.3    Ketchem, R.R.4    Narhi, L.O.5    Wypych, J.6
  • 27
  • 28
    • 60649093469 scopus 로고    scopus 로고
    • Mass spectrometry analysis of photo-induced methionine oxidation of a recombinant human monoclonal antibody
    • Liu H, Gaza-Bulseco G, Zhou L,. 2009. Mass spectrometry analysis of photo-induced methionine oxidation of a recombinant human monoclonal antibody. J Am Soc Mass Spectrom 20 (3): 525-528.
    • (2009) J am Soc Mass Spectrom , vol.20 , Issue.3 , pp. 525-528
    • Liu, H.1    Gaza-Bulseco, G.2    Zhou, L.3
  • 29
    • 0027791511 scopus 로고
    • Orthoclone OKT3. Chemical mechanisms and functional effects of degradation of a therapeutic monoclonal antibody
    • Rao PE, Kroon DJ,. 1993. Orthoclone OKT3. Chemical mechanisms and functional effects of degradation of a therapeutic monoclonal antibody. Pharm Biotechnol 5: 135-158.
    • (1993) Pharm Biotechnol , vol.5 , pp. 135-158
    • Rao, P.E.1    Kroon, D.J.2
  • 30
    • 84859312740 scopus 로고    scopus 로고
    • Oxidation of human growth hormone by oxygen-centered radicals: Formation of Leu-101 hydroperoxide and Tyr-103 oxidation products
    • Steinmann D, Ji JA, Wang YJ, Schoneich C,. 2012. Oxidation of human growth hormone by oxygen-centered radicals: Formation of Leu-101 hydroperoxide and Tyr-103 oxidation products. Mol Pharm 9 (4): 803-814.
    • (2012) Mol Pharm , vol.9 , Issue.4 , pp. 803-814
    • Steinmann, D.1    Ji, J.A.2    Wang, Y.J.3    Schoneich, C.4
  • 31
    • 84897992917 scopus 로고    scopus 로고
    • Screening methods to identify indole derivatives that protect against reactive oxygen species induced tryptophan oxidation in proteins
    • Grewal P, Mallaney M, Lau K, Sreedhara A,. 2014. Screening methods to identify indole derivatives that protect against reactive oxygen species induced tryptophan oxidation in proteins. Mol Pharm 11 (4): 1259-1272.
    • (2014) Mol Pharm , vol.11 , Issue.4 , pp. 1259-1272
    • Grewal, P.1    Mallaney, M.2    Lau, K.3    Sreedhara, A.4
  • 32
    • 79958838317 scopus 로고    scopus 로고
    • Analysis of 2,2′-azobis (2-amidinopropane) dihydrochloride degradation and hydrolysis in aqueous solutions
    • Werber J, Wang YJ, Milligan M, Li X, Ji JA,. 2011. Analysis of 2,2′-azobis (2-amidinopropane) dihydrochloride degradation and hydrolysis in aqueous solutions. J Pharm Sci 100 (8): 3307-3315.
    • (2011) J Pharm Sci , vol.100 , Issue.8 , pp. 3307-3315
    • Werber, J.1    Wang, Y.J.2    Milligan, M.3    Li, X.4    Ji, J.A.5
  • 33
    • 84897562208 scopus 로고    scopus 로고
    • Understanding the conformational impact of chemical modifications on monoclonal antibodies with diverse sequence variation using hydrogen/deuterium exchange mass spectrometry and structural modeling
    • Zhang A, Hu P, MacGregor P, Xue Y, Fan H, Suchecki P, Olszewski L, Liu A,. 2014. Understanding the conformational impact of chemical modifications on monoclonal antibodies with diverse sequence variation using hydrogen/deuterium exchange mass spectrometry and structural modeling. Anal Chem 86 (7): 3468-3475.
    • (2014) Anal Chem , vol.86 , Issue.7 , pp. 3468-3475
    • Zhang, A.1    Hu, P.2    MacGregor, P.3    Xue, Y.4    Fan, H.5    Suchecki, P.6    Olszewski, L.7    Liu, A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.