메뉴 건너뛰기




Volumn 9, Issue 6, 2005, Pages 555-560

Site-specific polymer modification of therapeutic proteins

Author keywords

[No Author keywords available]

Indexed keywords

RANTES; RECOMBINANT GRANULOCYTE COLONY STIMULATING FACTOR; RECOMBINANT PROTEIN;

EID: 27744530542     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2005.10.007     Document Type: Review
Times cited : (73)

References (59)
  • 1
    • 11144334098 scopus 로고    scopus 로고
    • Recombinant protein therapeutics- success rates, market trends and values to 2010
    • A.K. Pavlou, and J.M. Reichert Recombinant protein therapeutics- success rates, market trends and values to 2010 Nat Biotechnol 22 2004 1513 1519
    • (2004) Nat Biotechnol , vol.22 , pp. 1513-1519
    • Pavlou, A.K.1    Reichert, J.M.2
  • 2
    • 0346216863 scopus 로고    scopus 로고
    • Chemical and biological properties of polymer-modified proteins
    • G.G. Kochendoerfer Chemical and biological properties of polymer-modified proteins Expert Opin Biol Ther 3 2003 1253 1261
    • (2003) Expert Opin Biol Ther , vol.3 , pp. 1253-1261
    • Kochendoerfer, G.G.1
  • 3
    • 0037362655 scopus 로고    scopus 로고
    • Effect of pegylation on pharmaceuticals
    • J.M. Harris, and R.B. Chess Effect of pegylation on pharmaceuticals Nat Rev Drug Discov 2 2003 214 221 Excellent review of protein PEGylation, and its clinical application. The structure and development paths of major approved polymer-modified proteins are discussed.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 4
    • 0038387390 scopus 로고    scopus 로고
    • The Dawning era of polymer therapeutics
    • R. Duncan The Dawning era of polymer therapeutics Nat Rev Drug Discov 2 2003 347 360 Excellent review of the application of polymers to drug delivery.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 347-360
    • Duncan, R.1
  • 5
    • 0023683508 scopus 로고
    • Relationship of effective molecular size to systemic clearance in rats of recombinant interleukin-2 chemically modified with water-soluble polymers
    • M.J. Knauf, D.P. Bell, P. Hirtzer, Z.P. Luo, J.D. Young, and N.V. Katre Relationship of effective molecular size to systemic clearance in rats of recombinant interleukin-2 chemically modified with water-soluble polymers J Biol Chem 263 1988 15064 15070
    • (1988) J Biol Chem , vol.263 , pp. 15064-15070
    • Knauf, M.J.1    Bell, D.P.2    Hirtzer, P.3    Luo, Z.P.4    Young, J.D.5    Katre, N.V.6
  • 6
    • 0033654389 scopus 로고    scopus 로고
    • Modulation of the pharmacokinetics and pharmacodynamics of proteins by polyethylene glycol conjugation
    • R. Mehvar Modulation of the pharmacokinetics and pharmacodynamics of proteins by polyethylene glycol conjugation J Pharm Pharm Sci 3 2000 125 136
    • (2000) J Pharm Pharm Sci , vol.3 , pp. 125-136
    • Mehvar, R.1
  • 8
    • 0017701219 scopus 로고
    • Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol
    • A. Abuchowski, T. Van Es, N.C. Palczuk, and F.F. Davis 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
    • 0025128987 scopus 로고
    • Immunogenicity of recombinant IL-2 modified by covalent attachment of polyethylene glycol
    • N.V. Katre Immunogenicity of recombinant IL-2 modified by covalent attachment of polyethylene glycol J Immunol 144 1990 209 213
    • (1990) J Immunol , vol.144 , pp. 209-213
    • Katre, N.V.1
  • 10
    • 0026124772 scopus 로고
    • The therapeutic value of polyethylene glycol-modified proteins
    • M.L. Nucci, R. Shorr, and A. Abuchowski The therapeutic value of polyethylene glycol-modified proteins Adv Drug Deliv Rev 6 1991 133 151
    • (1991) Adv Drug Deliv Rev , vol.6 , pp. 133-151
    • Nucci, M.L.1    Shorr, R.2    Abuchowski, A.3
  • 11
    • 0001365675 scopus 로고
    • Chemical modification of recombinant interleukin 2 by polyethylene glycol increases its potency in the murine Meth a sarcoma model
    • N.V. Katre, M.J. Knauf, and W.J. Laird Chemical modification of recombinant interleukin 2 by polyethylene glycol increases its potency in the murine Meth A sarcoma model Proc Natl Acad Sci USA 84 1987 1487 1491
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1487-1491
    • Katre, N.V.1    Knauf, M.J.2    Laird, W.J.3
  • 12
    • 0035086519 scopus 로고    scopus 로고
    • Rational design of a potent, long-lasting form of interferon: A 40 kDa branched polyethylene glycol-conjugated interferon α-2a for the treatment of hepatitis C
    • P. Bailon, A. Palleroni, C.A. Schaffer, C.L. Spence, W.J. Fung, J.E. Porter, G.K. Ehrlich, W. Pan, Z.X. Xu, and M.W. Modi Rational design of a potent, long-lasting form of interferon: a 40 kDa branched polyethylene glycol-conjugated interferon α-2a for the treatment of hepatitis C Bioconjug Chem 12 2001 195 202
    • (2001) Bioconjug Chem , vol.12 , pp. 195-202
    • Bailon, P.1    Palleroni, A.2    Schaffer, C.A.3    Spence, C.L.4    Fung, W.J.5    Porter, J.E.6    Ehrlich, G.K.7    Pan, W.8    Xu, Z.X.9    Modi, M.W.10
  • 13
    • 0028343321 scopus 로고
    • Modification of recombinant human granulocyte colony-stimulating factor (rhG-CSF) and its derivative ND 28 with polyethylene glycol
    • M. Yamasaki, M. Asano, M. Okabe, M. Morimoto, and Y. Yokoo Modification of recombinant human granulocyte colony-stimulating factor (rhG-CSF) and its derivative ND 28 with polyethylene glycol J Biochem (Tokyo) 115 1994 814 819
    • (1994) J Biochem (Tokyo) , vol.115 , pp. 814-819
    • Yamasaki, M.1    Asano, M.2    Okabe, M.3    Morimoto, M.4    Yokoo, Y.5
  • 16
    • 0032146861 scopus 로고    scopus 로고
    • Chemical protein synthesis
    • J. Wilken, and S.B.H. Kent Chemical protein synthesis Curr Opin Biotechnol 9 1998 412 426 Excellent review of the history of chemoselective ligation approaches.
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 412-426
    • Wilken, J.1    Kent, S.B.H.2
  • 18
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • P.E. Dawson, and S.B.H. Kent Synthesis of native proteins by chemical ligation Annu Rev Biochem 69 2000 923 962
    • (2000) Annu Rev Biochem , vol.69 , pp. 923-962
    • Dawson, P.E.1    Kent, S.B.H.2
  • 19
    • 0345742616 scopus 로고    scopus 로고
    • A new strategy for the synthesis of glycoproteins
    • Z. Zhang, J. Gildersleeve, Y-Y. Yang, R. Xu, J.A. Loo, S. Uryu, C-H. Wong, and P.G. Schultz A new strategy for the synthesis of glycoproteins Science 303 2004 371 373 Site-specific incorporation of glyco-amino acid building blocks into recombinant proteins in E. coli.
    • (2004) Science , vol.303 , pp. 371-373
    • Zhang, Z.1    Gildersleeve, J.2    Yang, Y.-Y.3    Xu, R.4    Loo, J.A.5    Uryu, S.6    Wong, C.-H.7    Schultz, P.G.8
  • 21
    • 0345549549 scopus 로고    scopus 로고
    • Non-canonical amino acids in protein engineering
    • A.J. Link, M.L. Mock, and D.A. Tirrell Non-canonical amino acids in protein engineering Curr Opin Biotechnol 14 2003 603 609
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 603-609
    • Link, A.J.1    Mock, M.L.2    Tirrell, D.A.3
  • 26
    • 0034913652 scopus 로고    scopus 로고
    • Filgrastim (r-metHuG-CSF) in the 21st century: SD/01
    • G. Morstyn, M.A. Foote, T. Walker, and G. Molineux Filgrastim (r-metHuG-CSF) in the 21st century: SD/01 Acta Haematol 105 2001 151 155
    • (2001) Acta Haematol , vol.105 , pp. 151-155
    • Morstyn, G.1    Foote, M.A.2    Walker, T.3    Molineux, G.4
  • 27
    • 0028231302 scopus 로고
    • Facile synthesis of homogeneous artificial proteins
    • K. Rose Facile synthesis of homogeneous artificial proteins J Am Chem Soc 116 1994 30 33
    • (1994) J Am Chem Soc , vol.116 , pp. 30-33
    • Rose, K.1
  • 28
    • 0036000120 scopus 로고    scopus 로고
    • Total chemical synthesis of a 27 kDa TASP protein derived from the MscL ion channel of M. tuberculosis by ketoxime-forming ligation
    • G.G. Kochendoerfer, J.M. Tack, and S. Cressman Total chemical synthesis of a 27 kDa TASP protein derived from the MscL ion channel of M. tuberculosis by ketoxime-forming ligation Bioconjug Chem 13 2002 474 480
    • (2002) Bioconjug Chem , vol.13 , pp. 474-480
    • Kochendoerfer, G.G.1    Tack, J.M.2    Cressman, S.3
  • 29
    • 0030059104 scopus 로고    scopus 로고
    • Site-specific attachment of functionalized poly(ethylene glycol) to the amino terminus of proteins
    • H.F. Gaertner, and R.E. Offord Site-specific attachment of functionalized poly(ethylene glycol) to the amino terminus of proteins Bioconjug Chem 7 1996 38 44
    • (1996) Bioconjug Chem , vol.7 , pp. 38-44
    • Gaertner, H.F.1    Offord, R.E.2
  • 30
    • 0026857064 scopus 로고
    • Construction of protein analogs by site-specific condensation of unprotected fragments
    • H.F. Gaertner, K. Rose, R. Cotton, D. Timms, R. Camble, and R.E. Offord Construction of protein analogs by site-specific condensation of unprotected fragments Bioconjug Chem 3 1992 262 268
    • (1992) Bioconjug Chem , vol.3 , pp. 262-268
    • Gaertner, H.F.1    Rose, K.2    Cotton, R.3    Timms, D.4    Camble, R.5    Offord, R.E.6
  • 31
    • 0037423148 scopus 로고    scopus 로고
    • Design and chemical synthesis of a homogeneous polymer-modified erythropoiesis protein
    • G.G. Kochendoerfer, S.Y. Chen, F. Mao, S. Cressman, S. Traviglia, H. Shao, C.L. Hunter, D.W. Low, E.N. Cagle, and M. Carnevali Design and chemical synthesis of a homogeneous polymer-modified erythropoiesis protein Science 299 2003 884 887 Total synthesis of a 51 kDa protein-polymer conjugate by purely chemical means. This protein product candidate has entered Phase 1 clinical trials.
    • (2003) Science , vol.299 , pp. 884-887
    • Kochendoerfer, G.G.1    Chen, S.Y.2    Mao, F.3    Cressman, S.4    Traviglia, S.5    Shao, H.6    Hunter, C.L.7    Low, D.W.8    Cagle, E.N.9    Carnevali, M.10
  • 34
    • 27744463965 scopus 로고    scopus 로고
    • Polymer Conjugates of Interferon-beta With Enhanced Biological Potency. PCT Publication WO 2004/0126361.
    • Saifer MGP, Martinez AL, Williams LD, Sherman MR: Polymer Conjugates of Interferon-beta With Enhanced Biological Potency. PCT Publication WO 2004/0126361.
    • Saifer, M.G.P.1    Martinez, A.L.2    Williams, L.D.3    Sherman, M.R.4
  • 35
    • 27744499573 scopus 로고    scopus 로고
    • Methods and Kits for Making Polypeptides Having a Single Covalently Bound N-terminal Water-Soluble Polymer. US Patent 2000, 6,077,939.
    • Wei Z, Menon-Rudolph S, Ghosh-Dastidar P: Methods and Kits for Making Polypeptides Having a Single Covalently Bound N-terminal Water-Soluble Polymer. US Patent 2000, 6,077,939.
    • Wei, Z.1    Menon-Rudolph, S.2    Ghosh-Dastidar, P.3
  • 36
    • 0029787761 scopus 로고    scopus 로고
    • Site-specific protein modification using a ketone handle
    • V.W. Cornish, K.M. Hahn, and P.G. Schultz Site-specific protein modification using a ketone handle J Am Chem Soc 118 1996 8150 8151
    • (1996) J Am Chem Soc , vol.118 , pp. 8150-8151
    • Cornish, V.W.1    Hahn, K.M.2    Schultz, P.G.3
  • 37
    • 0037422608 scopus 로고    scopus 로고
    • Addition of the keto functional group to the genetic code of Escherichia coli
    • L. Wang, Z. Zhang, A. Brock, and P.G. Schultz Addition of the keto functional group to the genetic code of Escherichia coli Proc Natl Acad Sci USA 100 2003 56 61 Addition of the ketone functionality to proteins in E. coli enables the recombinant production of pharmaceutical proteins for subsequent site-specific polymer attachment.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 56-61
    • Wang, L.1    Zhang, Z.2    Brock, A.3    Schultz, P.G.4
  • 38
    • 0034677879 scopus 로고    scopus 로고
    • Cell surface engineering by a modified Staudinger reaction
    • E. Saxon, and C.R. Bertozzi Cell surface engineering by a modified Staudinger reaction Science 287 2000 2007 2010
    • (2000) Science , vol.287 , pp. 2007-2010
    • Saxon, E.1    Bertozzi, C.R.2
  • 39
    • 0034729576 scopus 로고    scopus 로고
    • Staudinger ligation: A peptide from a thioester and azide
    • B.L. Nilsson, L.L. Kiessling, and R.T. Raines Staudinger ligation: a peptide from a thioester and azide Org Lett 2 2000 1939 1941
    • (2000) Org Lett , vol.2 , pp. 1939-1941
    • Nilsson, B.L.1    Kiessling, L.L.2    Raines, R.T.3
  • 40
    • 0034643993 scopus 로고    scopus 로고
    • A "traceless" Staudinger ligation for the chemoselective synthesis of amide bonds
    • E. Saxon, J.I. Armstrong, and C.R. Bertozzi A "traceless" Staudinger ligation for the chemoselective synthesis of amide bonds Org Lett 2 2000 2141 2143
    • (2000) Org Lett , vol.2 , pp. 2141-2143
    • Saxon, E.1    Armstrong, J.I.2    Bertozzi, C.R.3
  • 41
    • 4644256655 scopus 로고    scopus 로고
    • C-terminal site-specific PEGylation of a truncated thrombomodulin mutant with retention of full bioactivity
    • C.S. Cazalis, C.A. Haller, L. Sease-Cargo, and E.L. Chaikof C-terminal site-specific PEGylation of a truncated thrombomodulin mutant with retention of full bioactivity Bioconjug Chem 15 2004 1005 1009
    • (2004) Bioconjug Chem , vol.15 , pp. 1005-1009
    • Cazalis, C.S.1    Haller, C.A.2    Sease-Cargo, L.3    Chaikof, E.L.4
  • 43
    • 7044260692 scopus 로고    scopus 로고
    • Site-specific PEGylation of proteins containing unnatural amino acids
    • A. Deiters, T.A. Cropp, D. Summerer, M. Mukherji, and P.G. Schultz Site-specific PEGylation of proteins containing unnatural amino acids Bioorg Med Chem Lett 14 2004 5743 5745 Site-specific PEG attachment to a recombinant protein via a specific linkage.
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 5743-5745
    • Deiters, A.1    Cropp, T.A.2    Summerer, D.3    Mukherji, M.4    Schultz, P.G.5
  • 44
  • 45
    • 0035804493 scopus 로고    scopus 로고
    • Native chemical ligation using removable N-α-(1-phenyl-2- mercaptoethyl) auxiliaries
    • P. Botti, M.R. Carrasco, and S.B.H. Kent Native chemical ligation using removable N-α-(1-phenyl-2-mercaptoethyl) auxiliaries Tet Lett 42 2001 1831 1833
    • (2001) Tet Lett , vol.42 , pp. 1831-1833
    • Botti, P.1    Carrasco, M.R.2    Kent, S.B.H.3
  • 46
    • 0036570182 scopus 로고    scopus 로고
    • Extending synthetic access to proteins with a removable acyl transfer auxiliary
    • J. Offer, Boddy CNC, and P.E. Dawson Extending synthetic access to proteins with a removable acyl transfer auxiliary J Am Chem Soc 124 2002 4642 4646
    • (2002) J Am Chem Soc , vol.124 , pp. 4642-4646
    • Offer, J.1    Cnc, B.2    Dawson, P.E.3
  • 47
    • 0035977638 scopus 로고    scopus 로고
    • Synthesis of peptides and proteins without cysteine residues by native chemical ligation combined with desulfurization
    • L. Yan, and P. Dawson Synthesis of peptides and proteins without cysteine residues by native chemical ligation combined with desulfurization J Am Chem Soc 123 2001 526 533
    • (2001) J Am Chem Soc , vol.123 , pp. 526-533
    • Yan, L.1    Dawson, P.2
  • 48
    • 1842738226 scopus 로고    scopus 로고
    • Total chemical synthesis and electrophysiological characterization of mechanosensitive channels from Escherichia coli and Mycobacterium tuberculosis
    • D. Clayton, G. Shapovalov, J.H. Maurer, D.A. Dougherty, H.A. Lester, and G.G. Kochendoerfer Total chemical synthesis and electrophysiological characterization of mechanosensitive channels from Escherichia coli and Mycobacterium tuberculosis Proc Natl Acad Sci USA 101 2004 4764 4769
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4764-4769
    • Clayton, D.1    Shapovalov, G.2    Maurer, J.H.3    Dougherty, D.A.4    Lester, H.A.5    Kochendoerfer, G.G.6
  • 50
    • 0032737391 scopus 로고    scopus 로고
    • Pharmacokinetics of novel erythropoiesis stimulating protein compared with epoetin alfa in dialysis patients
    • I.C. Macdougall, S.J. Gray, O. Elston, C. Breen, B. Jenkins, J. Browne, and J. Egrie Pharmacokinetics of novel erythropoiesis stimulating protein compared with epoetin alfa in dialysis patients J Am Soc Nephrol 10 1999 2392 2395
    • (1999) J Am Soc Nephrol , vol.10 , pp. 2392-2395
    • MacDougall, I.C.1    Gray, S.J.2    Elston, O.3    Breen, C.4    Jenkins, B.5    Browne, J.6    Egrie, J.7
  • 51
    • 0001083017 scopus 로고    scopus 로고
    • Aminooxy-, hydrazide-, and thiosemicarbazide-functionalized saccharides: Versatile reagents for glycoconjugate synthesis
    • E.C. Rodriguez, L.A. Marcaurelle, and C.R. Bertozzi Aminooxy-, hydrazide-, and thiosemicarbazide-functionalized saccharides: versatile reagents for glycoconjugate synthesis J Org Chem 63 1998 7134 7135
    • (1998) J Org Chem , vol.63 , pp. 7134-7135
    • Rodriguez, E.C.1    Marcaurelle, L.A.2    Bertozzi, C.R.3
  • 52
    • 0032511944 scopus 로고    scopus 로고
    • Synthesis of an oxime-linked neoglycopeptide with glycosylation-dependent activity similar to its native counterpart
    • L.A. Marcaurelle, E.C. Rodriguez, and C.R. Bertozzi Synthesis of an oxime-linked neoglycopeptide with glycosylation-dependent activity similar to its native counterpart Tet Lett 39 1998 8417 8420
    • (1998) Tet Lett , vol.39 , pp. 8417-8420
    • Marcaurelle, L.A.1    Rodriguez, E.C.2    Bertozzi, C.R.3
  • 53
    • 0035961527 scopus 로고    scopus 로고
    • Chemoselective elaboration of O-linked glycopeptide mimetics by alkylation of 3-thioGalNAc
    • L.A. Marcaurelle, and C.R. Bertozzi Chemoselective elaboration of O-linked glycopeptide mimetics by alkylation of 3-thioGalNAc J Am Chem Soc 123 2001 1587 1595
    • (2001) J Am Chem Soc , vol.123 , pp. 1587-1595
    • Marcaurelle, L.A.1    Bertozzi, C.R.2
  • 54
  • 55
    • 2542548800 scopus 로고    scopus 로고
    • Toward fully synthetic glycoproteins by ultimately convergent routes: A solution to a long-standing problem
    • J.D. Warren, J.S. Miller, S.J. Keding, and S.J. Danishefsky Toward fully synthetic glycoproteins by ultimately convergent routes: a solution to a long-standing problem J Am Chem Soc 126 2004 6576 6578
    • (2004) J Am Chem Soc , vol.126 , pp. 6576-6578
    • Warren, J.D.1    Miller, J.S.2    Keding, S.J.3    Danishefsky, S.J.4
  • 56
    • 0033596308 scopus 로고    scopus 로고
    • Fmoc-based synthesis of peptide-αthioesters: Application to the total chemical synthesis of a glycoprotein by native chemical ligation
    • Y. Shin, K. Winans, B. Backes, S. Kent, J. Ellman, and C. Bertozzi Fmoc-based synthesis of peptide-αthioesters: application to the total chemical synthesis of a glycoprotein by native chemical ligation J Am Chem Soc 121 1999 11684 11689
    • (1999) J Am Chem Soc , vol.121 , pp. 11684-11689
    • Shin, Y.1    Winans, K.2    Backes, B.3    Kent, S.4    Ellman, J.5    Bertozzi, C.6
  • 57
    • 3543108674 scopus 로고    scopus 로고
    • Modular assembly of glycoproteins: Towards the synthesis of GlyCAM-1 by using expressed protein ligation
    • D. Macmillan, and C.R. Bertozzi Modular assembly of glycoproteins: towards the synthesis of GlyCAM-1 by using expressed protein ligation Angew Chem Int Ed Engl 43 2004 1355 1359
    • (2004) Angew Chem Int Ed Engl , vol.43 , pp. 1355-1359
    • MacMillan, D.1    Bertozzi, C.R.2
  • 58
    • 3543095202 scopus 로고    scopus 로고
    • Cyanogen bromide cleavage generates fragments suitable for expressed protein and glycoprotein ligation
    • D. Macmillan, and L. Arham Cyanogen bromide cleavage generates fragments suitable for expressed protein and glycoprotein ligation J Am Chem Soc 126 2004 9530 9531
    • (2004) J Am Chem Soc , vol.126 , pp. 9530-9531
    • MacMillan, D.1    Arham, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.