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Volumn 60, Issue 1, 2008, Pages 50-58

Formulation of Neulasta® (pegfilgrastim)

Author keywords

(pegfilgrastim); Formulation; Neulasta ; PEGylation; r metHuG CSF

Indexed keywords

DEGRADATION; PROTEINS; SURFACE ACTIVE AGENTS; THAWING;

EID: 36549084078     PISSN: 0169409X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.addr.2007.04.017     Document Type: Review
Times cited : (107)

References (55)
  • 2
    • 0027258762 scopus 로고
    • The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors
    • Hill C.P., Osslund T.D., and Eisenberg D. The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 5167-5171
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 5167-5171
    • Hill, C.P.1    Osslund, T.D.2    Eisenberg, D.3
  • 3
    • 9944264495 scopus 로고    scopus 로고
    • Common structural stability properties of 4-helical bundle cytokines: possible physiological and pharmaceutical consequences
    • Ricci M.S., and Brems D.N. Common structural stability properties of 4-helical bundle cytokines: possible physiological and pharmaceutical consequences. Curr. Pharm. Des. 10 (2004) 3901-3911
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 3901-3911
    • Ricci, M.S.1    Brems, D.N.2
  • 5
    • 0027138673 scopus 로고
    • Cysteine 17 of recombinant human granulocyte-colony stimulating factor is partially solvent-exposed
    • Arakawa T., Prestrelski S.J., Narhi L.O., Boone T.C., and Kenney W.C. Cysteine 17 of recombinant human granulocyte-colony stimulating factor is partially solvent-exposed. J. Protein Chem. 12 (1993) 525-531
    • (1993) J. Protein Chem. , vol.12 , pp. 525-531
    • Arakawa, T.1    Prestrelski, S.J.2    Narhi, L.O.3    Boone, T.C.4    Kenney, W.C.5
  • 6
    • 1842535270 scopus 로고    scopus 로고
    • The design and development of pegfilgrastim (PEG-rmetHuG-CSF, Neulasta)
    • Molineux G. The design and development of pegfilgrastim (PEG-rmetHuG-CSF, Neulasta). Curr. Pharm. Des. 10 (2004) 1235-1244
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 1235-1244
    • Molineux, G.1
  • 7
    • 0028024499 scopus 로고
    • Filgrastim. A review of its pharmacological properties and therapeutic efficacy in neutropenia
    • Frampton J.E., Lee C.R., and Faulds D. Filgrastim. A review of its pharmacological properties and therapeutic efficacy in neutropenia. Drugs 48 (1994) 731-760
    • (1994) Drugs , vol.48 , pp. 731-760
    • Frampton, J.E.1    Lee, C.R.2    Faulds, D.3
  • 8
    • 0017701219 scopus 로고
    • Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol
    • Abuchowski A., van Es T., Palczuk N.C., and Davis F.F. Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol. J. Biol. Chem. 252 (1977) 3578-3581
    • (1977) J. Biol. Chem. , vol.252 , pp. 3578-3581
    • Abuchowski, A.1    van Es, T.2    Palczuk, N.C.3    Davis, F.F.4
  • 9
    • 33749121585 scopus 로고    scopus 로고
    • Pharmacokinetic consequences of PEGylation
    • Hamidi M., Azadi A., and Rafiei P. Pharmacokinetic consequences of PEGylation. Drug Deliv. 13 (2006) 399-409
    • (2006) Drug Deliv. , vol.13 , pp. 399-409
    • Hamidi, M.1    Azadi, A.2    Rafiei, P.3
  • 10
    • 0035816168 scopus 로고    scopus 로고
    • PEG drugs: an overview
    • B Greenwald R. PEG drugs: an overview. J. Control Release 74 (2001) 159-171
    • (2001) J. Control Release , vol.74 , pp. 159-171
    • B Greenwald, R.1
  • 12
    • 0037362655 scopus 로고    scopus 로고
    • Effect of PEGylation on pharmaceuticals
    • Harris J., and Chess R.B. Effect of PEGylation on pharmaceuticals. Nat. Rev., Drug Discov. 2 (2003) 214-221
    • (2003) Nat. Rev., Drug Discov. , vol.2 , pp. 214-221
    • Harris, J.1    Chess, R.B.2
  • 15
    • 0028337034 scopus 로고
    • Distribution and tissue uptake of poly[ethylene glycol) with different molecular weights after intravenous administration to mice
    • Yamaoka T., Tabata Y., and Ikada Y. Distribution and tissue uptake of poly[ethylene glycol) with different molecular weights after intravenous administration to mice. J. Pharm. Sci. 83 (1994) 601-606
    • (1994) J. Pharm. Sci. , vol.83 , pp. 601-606
    • Yamaoka, T.1    Tabata, Y.2    Ikada, Y.3
  • 18
    • 9244221679 scopus 로고    scopus 로고
    • Prediction of the viscosity radius and the size exclusion chromatography behavior of PEGylated proteins
    • Fee C.J., and Van Alstine J.M. Prediction of the viscosity radius and the size exclusion chromatography behavior of PEGylated proteins. Bioconjug. Chem. 15 (2004) 1304-1313
    • (2004) Bioconjug. Chem. , vol.15 , pp. 1304-1313
    • Fee, C.J.1    Van Alstine, J.M.2
  • 19
    • 0038243775 scopus 로고    scopus 로고
    • Pegfilgrastim: using PEGylation technology to improve neutropenia support in cancer patients
    • Molineux G. Pegfilgrastim: using PEGylation technology to improve neutropenia support in cancer patients. Anticancer Drugs 14 (2003) 259-264
    • (2003) Anticancer Drugs , vol.14 , pp. 259-264
    • Molineux, G.1
  • 20
    • 0036087485 scopus 로고    scopus 로고
    • Novel effects with polyethylene glycol modified pharmaceuticals
    • Yowell S.L., and Blackwell S. Novel effects with polyethylene glycol modified pharmaceuticals. Cancer Treat. Rev. 28 Suppl A (2002) 3-6
    • (2002) Cancer Treat. Rev. , vol.28 , Issue.SUPPL. A , pp. 3-6
    • Yowell, S.L.1    Blackwell, S.2
  • 21
    • 36549022463 scopus 로고    scopus 로고
    • Amgen, Inc., NEULASTA® (pegfilgrastim) Prescribing Information (2006).
  • 22
    • 0036267344 scopus 로고    scopus 로고
    • Pegfilgrastim
    • (discussion 1214-5)
    • Curran M.P., and Goa K.L. Pegfilgrastim. Drugs 62 (2002) 1207-1213 (discussion 1214-5)
    • (2002) Drugs , vol.62 , pp. 1207-1213
    • Curran, M.P.1    Goa, K.L.2
  • 23
    • 30344451118 scopus 로고    scopus 로고
    • Spotlight on pegfilgrastim in chemotherapy-induced neutropenia
    • Frampton J.E., and Keating G.M. Spotlight on pegfilgrastim in chemotherapy-induced neutropenia. BioDrugs 19 (2005) 405-407
    • (2005) BioDrugs , vol.19 , pp. 405-407
    • Frampton, J.E.1    Keating, G.M.2
  • 24
    • 36549075463 scopus 로고    scopus 로고
    • O.B. Kinstler, N.E. Gabriel, C.E. Farrar, R.B. DePrince, N-terminally Chemically Modified Protein Compositions and Methods (1999) US Patent 5985265, Amgen Inc.
  • 25
    • 0031588747 scopus 로고    scopus 로고
    • Ethanol-sodium chloride-phosphate mobile phase for size exclusion chromatography of poly(ethylene glycol) modified proteins
    • Ratto J., O'Conner S., Distler A., Wu G., Hummel D., Treuheit M., Herman A., and Davis J. Ethanol-sodium chloride-phosphate mobile phase for size exclusion chromatography of poly(ethylene glycol) modified proteins. J. Chromatgr., A 763 (1996) 337-344
    • (1996) J. Chromatgr., A , vol.763 , pp. 337-344
    • Ratto, J.1    O'Conner, S.2    Distler, A.3    Wu, G.4    Hummel, D.5    Treuheit, M.6    Herman, A.7    Davis, J.8
  • 28
    • 36549005402 scopus 로고    scopus 로고
    • O.B Kinstler, N.E Gabriel, C.E Farrar, R.B DePrince, N-terminally Chemically Modified Protein Compositions and Methods (1998) US Patent 5824784. Amgen Inc.
  • 32
    • 0025734440 scopus 로고
    • Conformational changes of recombinant human granulocyte-colony stimulating factor induced by pH and guanidine hydrochloride
    • Narhi L.O., Kenney W.C., and Arakawa T. Conformational changes of recombinant human granulocyte-colony stimulating factor induced by pH and guanidine hydrochloride. J. Protein Chem. 10 (1991) 359-367
    • (1991) J. Protein Chem. , vol.10 , pp. 359-367
    • Narhi, L.O.1    Kenney, W.C.2    Arakawa, T.3
  • 33
    • 0242432378 scopus 로고    scopus 로고
    • pH Dependence of structural stability of interleukin-2 and granulocyte colony-stimulating factor
    • Ricci M.S., Sarkar C.A., Fallon E.M., Lauffenburger D.A., and Brems D.N. pH Dependence of structural stability of interleukin-2 and granulocyte colony-stimulating factor. Protein Sci. 12 (2003) 1030-1038
    • (2003) Protein Sci. , vol.12 , pp. 1030-1038
    • Ricci, M.S.1    Sarkar, C.A.2    Fallon, E.M.3    Lauffenburger, D.A.4    Brems, D.N.5
  • 36
    • 0036784643 scopus 로고    scopus 로고
    • The kinetics of G-CSF folding
    • Brems D.N. The kinetics of G-CSF folding. Protein Sci. 11 (2002) 2504-2511
    • (2002) Protein Sci. , vol.11 , pp. 2504-2511
    • Brems, D.N.1
  • 39
    • 23844447975 scopus 로고    scopus 로고
    • Mechanism of protein stabilization by sugars during freeze-drying and storage: native structure preservation, specific interaction, and/or immobilization in a glassy matrix?
    • Chang L.L., Shepherd D., Sun J., Ouellette D., Grant K.L., Tang X.C., and Pikal M.J. Mechanism of protein stabilization by sugars during freeze-drying and storage: native structure preservation, specific interaction, and/or immobilization in a glassy matrix?. J. Pharm. Sci. 94 (2005) 1427-1444
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1427-1444
    • Chang, L.L.1    Shepherd, D.2    Sun, J.3    Ouellette, D.4    Grant, K.L.5    Tang, X.C.6    Pikal, M.J.7
  • 40
    • 0030712895 scopus 로고    scopus 로고
    • Phase separation of excipients during lyophilization: effects on protein stability
    • Randolph T.W. Phase separation of excipients during lyophilization: effects on protein stability. J. Pharm. Sci. 86 (1997) 1198-1203
    • (1997) J. Pharm. Sci. , vol.86 , pp. 1198-1203
    • Randolph, T.W.1
  • 41
    • 33845410077 scopus 로고    scopus 로고
    • Sorbitol crystallization can lead to protein aggregation in frozen protein formulations
    • Piedmonte D.M., Summers C., McAuley A., Karamujic L., and Ratnaswamy G. Sorbitol crystallization can lead to protein aggregation in frozen protein formulations. Pharm. Res. 24 (2007) 136-146
    • (2007) Pharm. Res. , vol.24 , pp. 136-146
    • Piedmonte, D.M.1    Summers, C.2    McAuley, A.3    Karamujic, L.4    Ratnaswamy, G.5
  • 42
    • 17644388499 scopus 로고    scopus 로고
    • Effects of excipients on the hydrogen peroxide-induced oxidation of methionine residues in granulocyte colony-stimulating factor
    • Yin J., Chu J.W., Ricci M.S., Brems D.N., Wang D.I., and Trout B.L. Effects of excipients on the hydrogen peroxide-induced oxidation of methionine residues in granulocyte colony-stimulating factor. Pharm. Res. 22 (2005) 141-147
    • (2005) Pharm. Res. , vol.22 , pp. 141-147
    • Yin, J.1    Chu, J.W.2    Ricci, M.S.3    Brems, D.N.4    Wang, D.I.5    Trout, B.L.6
  • 43
    • 0036111474 scopus 로고    scopus 로고
    • Inverse relationship of protein concentration and aggregation
    • Treuheit M.J., Kosky A.A., and Brems D.N. Inverse relationship of protein concentration and aggregation. Pharm. Res. 19 (2002) 511-516
    • (2002) Pharm. Res. , vol.19 , pp. 511-516
    • Treuheit, M.J.1    Kosky, A.A.2    Brems, D.N.3
  • 45
    • 0030443567 scopus 로고    scopus 로고
    • Surface-induced denaturation of proteins during freezing and its inhibition by surfactants
    • Chang B.S., Kendrick B.S., and Carpenter J.F. Surface-induced denaturation of proteins during freezing and its inhibition by surfactants. J. Pharm. Sci. 85 (1996) 1325-1330
    • (1996) J. Pharm. Sci. , vol.85 , pp. 1325-1330
    • Chang, B.S.1    Kendrick, B.S.2    Carpenter, J.F.3
  • 50
    • 0036784668 scopus 로고    scopus 로고
    • Peroxide formation in polysorbate 80 and protein stability
    • Ha E., Wang W., and Wang Y.J. Peroxide formation in polysorbate 80 and protein stability. J. Pharm. Sci. 91 (2002) 2252-2264
    • (2002) J. Pharm. Sci. , vol.91 , pp. 2252-2264
    • Ha, E.1    Wang, W.2    Wang, Y.J.3
  • 51
    • 36549085433 scopus 로고    scopus 로고
    • European Directorate for the Quality of Medicines, Council of Europe. Polysorbate 80. In: European Pharmacopoeia, 5th ed. Strasbourg, France. 04/2006:0428.
  • 52
    • 36549002571 scopus 로고    scopus 로고
    • O.B. Kinstler, N-terminally Chemically Modified Protein Compositions and Methods (2005) US Patent 6956027B2, Amgen Inc.
  • 53
    • 3042761213 scopus 로고    scopus 로고
    • Structure-immunogenicity relationships of therapeutic proteins
    • Hermeling S., Crommelin D.J., Schellekens H., and Jiskoot W. Structure-immunogenicity relationships of therapeutic proteins. Pharm. Res. 21 (2004) 897-903
    • (2004) Pharm. Res. , vol.21 , pp. 897-903
    • Hermeling, S.1    Crommelin, D.J.2    Schellekens, H.3    Jiskoot, W.4
  • 54
    • 0036890997 scopus 로고    scopus 로고
    • Immune responses to therapeutic proteins in humans-clinical significance, assessment and prediction
    • Koren E., Zuckerman L.A., and Mire-Sluis A.R. Immune responses to therapeutic proteins in humans-clinical significance, assessment and prediction. Curr. Pharm. Biotechnol. 3 (2002) 349-360
    • (2002) Curr. Pharm. Biotechnol. , vol.3 , pp. 349-360
    • Koren, E.1    Zuckerman, L.A.2    Mire-Sluis, A.R.3
  • 55
    • 32944459736 scopus 로고    scopus 로고
    • Factors influencing the immunogenicity of therapeutic proteins
    • Schellekens H. Factors influencing the immunogenicity of therapeutic proteins. Nephrol. Dial. Transplant. 20 Suppl 6 (2005) 3-9
    • (2005) Nephrol. Dial. Transplant. , vol.20 , Issue.SUPPL. 6 , pp. 3-9
    • Schellekens, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.