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Volumn 23, Issue 3, 2012, Pages 498-504

Using hydrogen/deuterium exchange mass spectrometry to study conformational changes in granulocyte colony stimulating factor upon PEGylation

Author keywords

Biopharmaceutical; Comparability; Polyethylene glycol; Posttranslational modification; Protein conformation; Therapeutic protein

Indexed keywords

BIOPHARMACEUTICAL; COMPARABILITY; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN CONFORMATION; THERAPEUTIC PROTEIN;

EID: 84860591482     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-011-0310-x     Document Type: Article
Times cited : (51)

References (35)
  • 1
    • 0017388651 scopus 로고
    • Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase
    • Abuchowski, A., McCoy, J.R., Palczuk, N.C., van Es, T., Davis, F.F.: Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase. J. Biol. Chem. 252, 3582-3586 (1977)
    • (1977) J. Biol. Chem. , vol.252 , pp. 3582-3586
    • Abuchowski, A.1    McCoy, J.R.2    Palczuk, N.C.3    Van Es, T.4    Davis, F.F.5
  • 3
    • 70349988803 scopus 로고    scopus 로고
    • PEG conjugates in clinical development or use as anticancer agents: An overview
    • Pasut, G., Veronese, F.M.: PEG conjugates in clinical development or use as anticancer agents: An overview. Adv. Drug Deliv. Rev. 61, 1177-1188 (2009)
    • (2009) Adv. Drug Deliv. Rev. , vol.61 , pp. 1177-1188
    • Pasut, G.1    Veronese, F.M.2
  • 4
    • 51549092094 scopus 로고    scopus 로고
    • The impact of PEGylation on biological therapies
    • Veronese, F.M., Mero, A.: The impact of PEGylation on biological therapies. BioDrugs 22, 315-329 (2008)
    • (2008) BioDrugs , vol.22 , pp. 315-329
    • Veronese, F.M.1    Mero, A.2
  • 5
    • 0033928514 scopus 로고    scopus 로고
    • Controlled-release, pegylation, liposomal formulations: New mechanisms in the delivery of injectable drugs
    • Reddy, K.R.: Controlled-release, pegylation, liposomal formulations: New mechanisms in the delivery of injectable drugs. Ann. Pharmacother. 34, 915-923 (2000)
    • (2000) Ann. Pharmacother. , vol.34 , pp. 915-923
    • Reddy, K.R.1
  • 6
    • 0037124466 scopus 로고    scopus 로고
    • PEGylated antibodies and antibody fragments for improved therapy: A review
    • Chapman, A.P.: PEGylated antibodies and antibody fragments for improved therapy: A review. Adv. Drug Deliv. Rev. 54, 531-545 (2002)
    • (2002) Adv. Drug Deliv. Rev. , vol.54 , pp. 531-545
    • Chapman, A.P.1
  • 7
    • 1342283696 scopus 로고    scopus 로고
    • Sodium dodecyl sulfate-capillary gel electrophoresis of polyethylene glycolylated interferon &uF061
    • Na, D.H., Park, E.J., Youn, Y.S., Moon, B.W., Jo, Y.W., Lee, S.H., Kim, W.B., Sohn, Y., Lee, K.C.: Sodium dodecyl sulfate-capillary gel electrophoresis of polyethylene glycolylated interferon &UF061. Electrophoresis 25, 476-479 (2004)
    • (2004) Electrophoresis , vol.25 , pp. 476-479
    • Na, D.H.1    Park, E.J.2    Youn, Y.S.3    Moon, B.W.4    Jo, Y.W.5    Lee, S.H.6    Kim, W.B.7    Sohn, Y.8    Lee, K.C.9
  • 8
    • 0037124398 scopus 로고    scopus 로고
    • Structural and biological characterization of pegylated recombinant interferon alpha-2b and its therapeutic implications
    • Wang, Y.S., Youngster, S., Grace, M., Bausch, J., Bordens, R., Wyss, D.F.: Structural and biological characterization of pegylated recombinant interferon alpha-2b and its therapeutic implications. Adv. Drug Deliv. Rev. 54, 547-570 (2002)
    • (2002) Adv. Drug Deliv. Rev. , vol.54 , pp. 547-570
    • Wang, Y.S.1    Youngster, S.2    Grace, M.3    Bausch, J.4    Bordens, R.5    Wyss, D.F.6
  • 9
    • 60549094223 scopus 로고    scopus 로고
    • Characterization of poly (ethylene glycol) and PEGylated products by LC/MS with postcolumn addition of amines
    • Huang, L., Gough, P.C., Defelippis, M.R.: Characterization of poly (ethylene glycol) and PEGylated products by LC/MS with postcolumn addition of amines. Anal. Chem. 81, 567-577 (2009)
    • (2009) Anal. Chem. , vol.81 , pp. 567-577
    • Huang, L.1    Gough, P.C.2    Defelippis, M.R.3
  • 11
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales, T.E., Engen, J.R.: Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev. 25, 158-170 (2006)
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 13
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Zhang, Z., Smith, D.L.: Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation. Protein Sci. 2, 522-531 (1993)
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 14
    • 67650757736 scopus 로고    scopus 로고
    • Characterization of IgG1 conformation and conformational dynamics by hydrogen/deuterium exchange mass spectrometry
    • Houde, D., Arndt, J., Domeier, W., Berkowitz, S., Engen, J.R.: Characterization of IgG1 conformation and conformational dynamics by hydrogen/deuterium exchange mass spectrometry. Anal. Chem. 81, 5966 (2009)
    • (2009) Anal. Chem. , vol.81 , pp. 5966
    • Houde, D.1    Arndt, J.2    Domeier, W.3    Berkowitz, S.4    Engen, J.R.5
  • 16
    • 0346431875 scopus 로고    scopus 로고
    • Probing Ca2+-induced conformational changes in porcine calmodulin by H/D exchange and ESI-MS: Effect of cations and ionic strength
    • Zhu, M.M., Rempel, D.L., Zhao, J., Giblin, D.E., Gross, M.L.: Probing Ca2+-induced conformational changes in porcine calmodulin by H/D exchange and ESI-MS: Effect of cations and ionic strength. Biochemistry 42, 15388-15397 (2003)
    • (2003) Biochemistry , vol.42 , pp. 15388-15397
    • Zhu, M.M.1    Rempel, D.L.2    Zhao, J.3    Giblin, D.E.4    Gross, M.L.5
  • 17
    • 0036102156 scopus 로고    scopus 로고
    • Epitope mapping of a monoclonal antibody against human thrombin by H/Dexchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein
    • Baerga-Ortiz, A., Hughes, C.A., Mandell, J.G., Komives, E.A.: Epitope mapping of a monoclonal antibody against human thrombin by H/Dexchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein. Protein Sci. 11, 1300-1308 (2002)
    • (2002) Protein Sci. , vol.11 , pp. 1300-1308
    • Baerga-Ortiz, A.1    Hughes, C.A.2    Mandell, J.G.3    Komives, E.A.4
  • 18
    • 62549108693 scopus 로고    scopus 로고
    • Epitope mapping by amide hydrogen/deuterium exchange coupled with immobilization of antibody, on-line proteolysis, liquid chromatography and mass spectrometry
    • Coales, S.J., Tuske, S.J., Tomasso, J.C., Hamuro, Y.: Epitope mapping by amide hydrogen/deuterium exchange coupled with immobilization of antibody, on-line proteolysis, liquid chromatography and mass spectrometry. Rapid Commun. Mass Spectrom. 23, 639-647 (2009)
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 639-647
    • Coales, S.J.1    Tuske, S.J.2    Tomasso, J.C.3    Hamuro, Y.4
  • 21
    • 6444222991 scopus 로고
    • Use of glass electrodes to measure acidities in deuterium oxide
    • Glasoe, P.K.: Use of glass electrodes to measure acidities in deuterium oxide. J. Phys. Chem. 64, 188-189 (1960)
    • (1960) J. Phys. Chem. , vol.64 , pp. 188-189
    • Glasoe, P.K.1
  • 22
    • 0027169975 scopus 로고
    • Isotope effects in peptide group hydrogen exchange
    • Connelly, G.P., Bai, Y., Jeng, M.F., Englander, S.W.: Isotope effects in peptide group hydrogen exchange. Proteins 17, 87-92 (1993)
    • (1993) Proteins , vol.17 , pp. 87-92
    • Connelly, G.P.1    Bai, Y.2    Jeng, M.F.3    Englander, S.W.4
  • 23
    • 51549121010 scopus 로고    scopus 로고
    • High-speed andhigh-resolution UPLC separation at zero degrees Celsius
    • Wales, T.E., Fadgen, K.E., Gerhardt, G.C., Engen, J.R.: High-speed andhigh-resolution UPLC separation at zero degrees Celsius. Anal Chem.80, 6815-6820 (2008)
    • (2008) Anal Chem. , vol.80 , pp. 6815-6820
    • Wales, T.E.1    Fadgen, K.E.2    Gerhardt, G.C.3    Engen, J.R.4
  • 24
    • 79954631167 scopus 로고    scopus 로고
    • False EX1 signaturescaused by sample carryover during HX MS analyses
    • Fang, J., Rand, K.D., Beuning, P.J., Engen, J.R.: False EX1 signaturescaused by sample carryover during HX MS analyses. Int. J. MassSpectrom. 302, 19-25 (2011)
    • (2011) Int. J. MassSpectrom. , vol.302 , pp. 19-25
    • Fang, J.1    Rand, K.D.2    Beuning, P.J.3    Engen, J.R.4
  • 25
    • 79954629044 scopus 로고    scopus 로고
    • MSTools-Web based application for visualizationand presentation of HXMS data
    • Kavana, D., Mana, P.: MSTools-Web based application for visualizationand presentation of HXMS data. Int. J. Mass. Spectrom. 302, 53-58 (2011)
    • (2011) Int. J. Mass. Spectrom. , vol.302 , pp. 53-58
    • Kavana, D.1    Mana, P.2
  • 26
    • 33751337111 scopus 로고    scopus 로고
    • Semi-automated data processing ofhydrogen exchange mass spectra using HX-Express
    • Weis, D.D., Engen, J.R., Kass, I.J.: Semi-automated data processing ofhydrogen exchange mass spectra using HX-Express. J. Am. Soc. Mass Spectrom. 17, 1700-1703 (2006)
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1700-1703
    • Weis, D.D.1    Engen, J.R.2    Kass, I.J.3
  • 27
    • 79954547968 scopus 로고    scopus 로고
    • The utility of hydrogen/ deuterium exchange mass spectrometry in biopharmaceutical comparability studies
    • Houde, D., Berkowitz, S.A., Engen, J.R.: The utility of hydrogen/ deuterium exchange mass spectrometry in biopharmaceutical comparability studies. J. Pharm. Sci. 100, 2071-2086 (2011)
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2071-2086
    • Houde, D.1    Berkowitz, S.A.2    Engen, J.R.3
  • 28
    • 60149083122 scopus 로고    scopus 로고
    • Assessment of the repeatability and reproducibility of hydrogen/deuterium exchange mass spectrometry measurements
    • Burkitt, W., O'Connor, G.: Assessment of the repeatability and reproducibility of hydrogen/deuterium exchange mass spectrometry measurements. Rapid Commun. Mass Spectrom. 22, 3893-3901 (2008)
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 3893-3901
    • Burkitt, W.1    O'Connor, G.2
  • 29
    • 33644761881 scopus 로고    scopus 로고
    • Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex
    • Tamada, T., Honjo, E., Maeda, Y., Okamoto, T., Ishibashi, M., Tokunaga, M., Kuroki, R.: Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex. Proc. Natl. Acad. Sci. U.S.A. 103, 3135-3140 (2006)
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 3135-3140
    • Tamada, T.1    Honjo, E.2    Maeda, Y.3    Okamoto, T.4    Ishibashi, M.5    Tokunaga, M.6    Kuroki, R.7
  • 31
    • 79955111543 scopus 로고    scopus 로고
    • Effects of HIV-1 Nef on human N-myristoyltransferase 1
    • Morgan, C.R., Miglionico, B.V., Engen, J.R.: Effects of HIV-1 Nef on human N-myristoyltransferase 1. Biochemistry 50, 3394-3403 (2011)
    • (2011) Biochemistry , vol.50 , pp. 3394-3403
    • Morgan, C.R.1    Miglionico, B.V.2    Engen, J.R.3
  • 32
    • 0036155132 scopus 로고    scopus 로고
    • Pegnology: A review of PEG-ylated systems
    • Bhadra, D., Bhadra, S., Jain, P., Jain, N.K.: Pegnology: A review of PEG-ylated systems. Pharmazie 57, 5-29 (2002)
    • (2002) Pharmazie , vol.57 , pp. 5-29
    • Bhadra, D.1    Bhadra, S.2    Jain, P.3    Jain, N.K.4
  • 34


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.