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Volumn 5, Issue , 2014, Pages

Semi-permeable coatings fabricated from comb-polymers efficiently protect proteins in vivo

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINASE; EPITOPE; POLYMER; ANTINEOPLASTIC AGENT; DRUG CARRIER; MACROGOL DERIVATIVE; METHACRYLIC ACID DERIVATIVE; POLYETHYLENE GLYCOL METHACRYLATE;

EID: 84923345372     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6526     Document Type: Article
Times cited : (59)

References (47)
  • 1
    • 0037362655 scopus 로고    scopus 로고
    • Effect of pegylation on pharmaceuticals
    • Harris, J. M. & Chess, R. B. Effect of pegylation on pharmaceuticals. Nat. Rev. Drug Discov. 2, 214-221 (2003).
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 2
    • 84861749627 scopus 로고    scopus 로고
    • State of the art in pegylation: The great versatility achieved after forty years of research
    • Pasut, G. & Veronese, F. M. State of the art in PEGylation: The great versatility achieved after forty years of research. J. Control. Release 161, 461-472 (2012).
    • (2012) J. Control. Release , vol.161 , pp. 461-472
    • Pasut, G.1    Veronese, F.M.2
  • 3
    • 80051753313 scopus 로고    scopus 로고
    • Fda-Approved poly(ethylene glycol)-protein conjugate drugs
    • Alconcel, S. N. S., Baas, A. S. & Maynard, H. D. FDA-Approved poly(ethylene glycol)-protein conjugate drugs. Polym. Chem. 2, 1442-1448 (2011).
    • (2011) Polym. Chem. , vol.2 , pp. 1442-1448
    • Alconcel, S.N.S.1    Baas, A.S.2    Maynard, H.D.3
  • 4
    • 0038387390 scopus 로고    scopus 로고
    • The dawning era of polymer therapeutics
    • Duncan, R. The dawning era of polymer therapeutics. Nat. Rev. Drug Discov. 2, 347-360 (2003).
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 347-360
    • Duncan, R.1
  • 5
    • 67949112461 scopus 로고    scopus 로고
    • Nanostructured functional materials prepared by atom transfer radical polymerization
    • Matyjaszewski, K. & Tsarevsky, N. V. Nanostructured functional materials prepared by atom transfer radical polymerization. Nat. Chem. 1, 276-288 (2009).
    • (2009) Nat. Chem. , vol.1 , pp. 276-288
    • Matyjaszewski, K.1    Tsarevsky, N.V.2
  • 6
    • 79951998821 scopus 로고    scopus 로고
    • Controlled folding of synthetic polymer chains through the formation of positionable covalent bridges
    • Schmidt BVKJ, Fechler N, Falkenhagen, J. & Lutz, J.-F. Controlled folding of synthetic polymer chains through the formation of positionable covalent bridges. Nat. Chem. 3, 234-238 (2011).
    • (2011) Nat. Chem. , vol.3 , pp. 234-238
    • Bvkj, S.1    Fechler, N.2    Falkenhagen, J.3    Lutz, J.-F.4
  • 7
    • 84858767015 scopus 로고    scopus 로고
    • A two-dimensional polymer prepared by organic synthesis
    • Kissel, P. et al. A two-dimensional polymer prepared by organic synthesis. Nat. Chem. 4, 287-291 (2012).
    • (2012) Nat. Chem. , vol.4 , pp. 287-291
    • Kissel, P.1
  • 8
    • 84875431729 scopus 로고    scopus 로고
    • A heparin-mimicking polymer conjugate stabilizes basic fibroblast growth factor
    • Nguyen, T. H. et al. A heparin-mimicking polymer conjugate stabilizes basic fibroblast growth factor. Nat. Chem. 5, 221-227 (2013).
    • (2013) Nat. Chem. , vol.5 , pp. 221-227
    • Nguyen, T.H.1
  • 9
    • 83655197598 scopus 로고    scopus 로고
    • Poly(zwitterionic) protein conjugates offer increased stability without sacrificing binding affinity or bioactivity
    • Keefe, A. J. & Jiang, S. Poly(zwitterionic)protein conjugates offer increased stability without sacrificing binding affinity or bioactivity. Nat. Chem. 4, 59-63 (2012).
    • (2012) Nat. Chem. , vol.4 , pp. 59-63
    • Keefe, A.J.1    Jiang, S.2
  • 10
    • 84879401007 scopus 로고    scopus 로고
    • Sustained gastrointestinal activity of dendronized polymer-enzyme conjugates
    • Fuhrmann, G. et al. Sustained gastrointestinal activity of dendronized polymer-enzyme conjugates. Nat. Chem. 5, 582-589 (2013).
    • (2013) Nat. Chem. , vol.5 , pp. 582-589
    • Fuhrmann, G.1
  • 11
    • 79959340087 scopus 로고    scopus 로고
    • In vivo fluorescence imaging of exogenous enzyme activity in the gastrointestinal tract
    • Fuhrmann, G. & Leroux, J.-C. In vivo fluorescence imaging of exogenous enzyme activity in the gastrointestinal tract. Proc. Natl Acad. Sci. USA 108, 9032-9037 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 9032-9037
    • Fuhrmann, G.1    Leroux, J.-C.2
  • 12
    • 84876225476 scopus 로고    scopus 로고
    • Molecular sieving on the surface of a protein provides protection without loss of activity
    • Liu, M. et al. Molecular Sieving on the Surface of a Protein Provides Protection Without Loss of Activity. Adv. Funct. Mater. 23, 2007-2015 (2013).
    • (2013) Adv. Funct. Mater. , vol.23 , pp. 2007-2015
    • Liu, M.1
  • 14
    • 0034791821 scopus 로고    scopus 로고
    • Pharmacokinetics of native escherichia coli asparaginase (asparaginase medac) and hypersensitivity reactions in all-bfm 95 reinduction treatment
    • Müller, H.-J. et al. Pharmacokinetics of native Escherichia coli asparaginase (Asparaginase medac) and hypersensitivity reactions in ALL-BFM 95 reinduction treatment. Br. J. Haematol. 114, 794-799 (2001).
    • (2001) Br. J. Haematol. , vol.114 , pp. 794-799
    • Müller, H.-J.1
  • 15
    • 2942677283 scopus 로고    scopus 로고
    • Asparaginase pharmacodynamics differ by formulation among children with newly diagnosed acute lymphoblastic leukemia
    • Hak, L. J. et al. Asparaginase pharmacodynamics differ by formulation among children with newly diagnosed acute lymphoblastic leukemia. Leukemia 18, 1072-1077 (2004).
    • (2004) Leukemia , vol.18 , pp. 1072-1077
    • Hak, L.J.1
  • 16
    • 0037085747 scopus 로고    scopus 로고
    • A randomized comparison of native escherichia coli asparaginase and polyethylene glycol conjugated asparaginase for treatment of children with newly diagnosed standard-risk acute lymphoblastic leukemia: A children's cancer group study
    • Avramis, V. I. et al. A randomized comparison of native Escherichia coli asparaginase and polyethylene glycol conjugated asparaginase for treatment of children with newly diagnosed standard-risk acute lymphoblastic leukemia: a Children's Cancer Group study. Blood 99, 1986-1994 (2002).
    • (2002) Blood , vol.99 , pp. 1986-1994
    • Avramis, V.I.1
  • 17
    • 0027197614 scopus 로고
    • Comparative pharmacokinetic studies of three asparaginase preparations
    • Asselin, B. L. et al. Comparative pharmacokinetic studies of three asparaginase preparations. J. Clin. Oncol. 11, 1780-1786 (1993).
    • (1993) J. Clin. Oncol. , vol.11 , pp. 1780-1786
    • Asselin, B.L.1
  • 18
    • 34250018555 scopus 로고    scopus 로고
    • Intensified peg-l-Asparaginase and antimetabolite-based therapy for treatment of higher risk precursor-b acute lymphoblastic leukemia: A report from the children's oncology group
    • Salzer, W. L. et al. Intensified PEG-L-Asparaginase and antimetabolite-based therapy for treatment of higher risk precursor-B acute lymphoblastic leukemia: a Report From the Children's Oncology Group. J. Pediatr. Hematol. Oncol. 29, 369-375 (2007).
    • (2007) J. Pediatr. Hematol. Oncol. , vol.29 , pp. 369-375
    • Salzer, W.L.1
  • 19
    • 77951706358 scopus 로고    scopus 로고
    • Therapeutic drug monitoring of asparaginase in the all-bfm 2000 protocol between 2000 and 2007 pediatr
    • Schrey, D. et al. Therapeutic drug monitoring of asparaginase in the ALL-BFM 2000 protocol between 2000 and 2007. Pediatr. Blood Cancer 54, 952-958 (2010).
    • (2010) Blood Cancer , vol.54 , pp. 952-958
    • Schrey, D.1
  • 20
    • 0017196587 scopus 로고
    • Small-Angle x-ray scattering studies of escherichia coli l-Asparaginase
    • Murthy, N. S. & Knox, J. R. Small-Angle X-ray scattering studies of Escherichia coli l-Asparaginase. J. Mol. Biol. 105, 567-575 (1976).
    • (1976) J. Mol. Biol. , vol.105 , pp. 567-575
    • Murthy, N.S.1    Knox, J.R.2
  • 21
    • 84866920418 scopus 로고    scopus 로고
    • Use of the interior cavity of the p22 capsid for site-specific initiation of atom-transfer radical polymerization with high-density cargo loading
    • Lucon, J. et al. Use of the interior cavity of the P22 capsid for site-specific initiation of atom-transfer radical polymerization with high-density cargo loading. Nat. Chem. 4, 781-788 (2012).
    • (2012) Nat. Chem. , vol.4 , pp. 781-788
    • Lucon, J.1
  • 23
    • 84880509608 scopus 로고    scopus 로고
    • Tailoring enzyme activity and stability using polymer-based protein engineering
    • Cummings, C., Murata, H., Koepsel, R. & Russell, A. J. Tailoring enzyme activity and stability using polymer-based protein engineering. Biomaterials 34, 7437-7443 (2013).
    • (2013) Biomaterials , vol.34 , pp. 7437-7443
    • Cummings, C.1    Murata, H.2    Koepsel, R.3    Russell, A.J.4
  • 24
    • 84878861673 scopus 로고    scopus 로고
    • Polymer-based protein engineering can rationally tune enzyme activity ph-dependence, and stability
    • Murata, H., Cummings, C. S., Koepsel, R. R. & Russell, A. J. Polymer-Based Protein Engineering Can Rationally Tune Enzyme Activity, pH-Dependence, and Stability. Biomacromolecules 14, 1919-1926 (2013).
    • (2013) Biomacromolecules , vol.14 , pp. 1919-1926
    • Murata, H.1    Cummings, C.S.2    Koepsel, R.R.3    Russell, A.J.4
  • 25
    • 84896771198 scopus 로고    scopus 로고
    • Dramatically increased ph and temperature stability of chymotrypsin using dual block polymer-based protein engineering
    • Cummings, C., Murata, H., Koepsel, R. & Russell, A. J. Dramatically increased pH and temperature stability of chymotrypsin using dual block polymer-based protein engineering. Biomacromolecules 15, 763-771 (2014).
    • (2014) Biomacromolecules , vol.15 , pp. 763-771
    • Cummings, C.1    Murata, H.2    Koepsel, R.3    Russell, A.J.4
  • 26
    • 61849119647 scopus 로고    scopus 로고
    • Small angle neutron scattering study of conformation of oligo(ethylene glycol)-grafted polystyrene in dilute solutions: Effect of the backbone length
    • Cheng, G. et al. Small angle neutron scattering study of conformation of oligo(ethylene glycol)-grafted polystyrene in dilute solutions: effect of the backbone length. Macromolecules 41, 9831-9836 (2008).
    • (2008) Macromolecules , vol.41 , pp. 9831-9836
    • Cheng, G.1
  • 27
    • 84859582352 scopus 로고    scopus 로고
    • Comparison between the lcst and ucst transitions of double thermoresponsive diblock copolymers: Insights into the behavior of poegma in alcohols
    • Roth, P. J., Davis, T. P. & Lowe, A. B. Comparison between the LCST and UCST transitions of double thermoresponsive diblock copolymers: insights into the behavior of POEGMA in alcohols. Macromolecules 45, 3221-3230 (2012).
    • (2012) Macromolecules , vol.45 , pp. 3221-3230
    • Roth, P.J.1    Davis, T.P.2    Lowe, A.B.3
  • 28
    • 0023864098 scopus 로고
    • Polyethylene glycol-l-Asparaginase and l-Asparaginase studies in rabbits
    • Ho, D. H. et al. Polyethylene glycol-L-Asparaginase and L-Asparaginase studies in rabbits. Drug Metab. Dispos. 16, 27-29 (1988).
    • (1988) Drug Metab. Dispos. , vol.16 , pp. 27-29
    • Ho, D.H.1
  • 29
    • 84867760417 scopus 로고    scopus 로고
    • Antibodies against polyethylene glycol in healthy subjects and in patients treated with peg-conjugated agents
    • Garay, R. P., El-Gewely, R., Armstrong, J. K., Garratty, G. & Richette, P. Antibodies against polyethylene glycol in healthy subjects and in patients treated with PEG-conjugated agents. Expert Opin. Drug Deliv. 9, 1319-1323 (2012).
    • (2012) Expert Opin. Drug Deliv. , vol.9 , pp. 1319-1323
    • Garay, R.P.1    El-Gewely, R.2    Armstrong, J.K.3    Garratty, G.4    Richette, P.5
  • 30
    • 34250800861 scopus 로고    scopus 로고
    • Antibody against poly(ethylene glycol) adversely affects peg-Asparaginase therapy in acute lymphoblastic leukemia patients
    • Armstrong, J. K. et al. Antibody against poly(ethylene glycol) adversely affects PEG-Asparaginase therapy in acute lymphoblastic leukemia patients. Cancer 110, 103-111 (2007).
    • (2007) Cancer , vol.110 , pp. 103-111
    • Armstrong, J.K.1
  • 31
    • 78649704670 scopus 로고    scopus 로고
    • Polymer-protein conjugates: An enzymatic activity perspective
    • Gauthier, M. A. & Klok, H.-A. Polymer-protein conjugates: an enzymatic activity perspective. Polym. Chem. 1, 1352-1373 (2010).
    • (2010) Polym. Chem. , vol.1 , pp. 1352-1373
    • Gauthier, M.A.1    Klok, H.-A.2
  • 32
    • 36549004553 scopus 로고    scopus 로고
    • Anti-cancer peg-enzymes: 30 years old, but still a current approach
    • Pasut, G., Sergi, M. & Veronese, F. M. Anti-cancer PEG-enzymes: 30 years old, but still a current approach. Adv. Drug Deliv. Rev. 60, 69-78 (2008).
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 69-78
    • Pasut, G.1    Sergi, M.2    Veronese, F.3
  • 33
    • 0029888326 scopus 로고    scopus 로고
    • Improvement of pharmacokinetic, immunological and stability properties of asparaginase by conjugation to linear and branched monomethoxy poly(ethylene glycol
    • Veronese, F. M. et al. Improvement of pharmacokinetic, immunological and stability properties of asparaginase by conjugation to linear and branched monomethoxy poly(ethylene glycol). J. Control. Release 40, 199-209 (1996).
    • (1996) J. Control. Release , vol.40 , pp. 199-209
    • Veronese, F.M.1
  • 34
    • 0029167706 scopus 로고
    • A branched monomethoxypoly(ethylene glycol) for protein modification
    • Monfardini, C. et al. A branched monomethoxypoly(ethylene glycol) for protein modification. Bioconjug. Chem. 6, 62-69 (1995).
    • (1995) Bioconjug. Chem. , vol.6 , pp. 62-69
    • Monfardini, C.1
  • 35
    • 33645319958 scopus 로고    scopus 로고
    • Surface-initiated atom transfer radical polymerization of oligo(ethylene glycol) methyl methacrylate from a mixed self-Assembled monolayer on gold
    • Ma, H., Wells, M., Beebe, T. P. & Chilkoti, A. Surface-initiated atom transfer radical polymerization of oligo(ethylene glycol) methyl methacrylate from a mixed self-Assembled monolayer on gold. Adv. Funct. Mater. 16, 640-648 (2006).
    • (2006) Adv. Funct. Mater. , vol.16 , pp. 640-648
    • Ma, H.1    Wells, M.2    Beebe, T.P.3    Chilkoti, A.4
  • 36
    • 1642263784 scopus 로고    scopus 로고
    • Non-fouling' oligo(ethylene glycol)-functionalized polymer brushes synthesized by surface-initiated atom transfer radical polymerization
    • Ma, H., Hyun, J., Stiller, P. & Chilkoti, A. 'Non-fouling' oligo(ethylene glycol)-functionalized polymer brushes synthesized by surface-initiated atom transfer radical polymerization. Adv. Mater. 16, 338-341 (2004).
    • (2004) Adv. Mater. , vol.16 , pp. 338-341
    • Ma, H.1    Hyun, J.2    Stiller, P.3    Chilkoti, A.4
  • 37
    • 77951267238 scopus 로고    scopus 로고
    • In situ growth of side-chain peg polymers from functionalized human growth hormone-A new technique for preparation of enhanced protein-polymer conjugates
    • Magnusson, J. P., Bersani, S., Salmaso, S., Alexander, C. & Caliceti, P. In situ growth of side-chain peg polymers from functionalized human growth hormone-A new technique for preparation of enhanced protein-polymer conjugates. Bioconjug. Chem. 21, 671-678 (2010).
    • (2010) Bioconjug. Chem. , vol.21 , pp. 671-678
    • Magnusson, J.P.1    Bersani, S.2    Salmaso, S.3    Alexander, C.4    Caliceti, P.5
  • 38
    • 78049256803 scopus 로고    scopus 로고
    • In situ growth of a peg-like polymer from the c terminus of an intein fusion protein improves pharmacokinetics and tumor accumulation
    • Gao, W. P., Liu, W. G., Christensen, T., Zalutsky, M. R. & Chilkoti, A. In situ growth of a PEG-like polymer from the C terminus of an intein fusion protein improves pharmacokinetics and tumor accumulation. Proc. Natl Acad. Sci. USA 107, 16432-16437 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 16432-16437
    • Gao, W.P.1    Liu, W.G.2    Christensen, T.3    Zalutsky, M.R.4    Chilkoti, A.5
  • 39
    • 70349339238 scopus 로고    scopus 로고
    • In situ growth of a stoichiometric peg-like conjugate at a protein's n-terminus with significantly improved pharmacokinetics
    • Gao, W. P. et al. In situ growth of a stoichiometric PEG-like conjugate at a protein's N-terminus with significantly improved pharmacokinetics. Proc. Natl Acad. Sci. USA 106, 15231-15236 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 15231-15236
    • Gao, W.P.1
  • 40
    • 61649092532 scopus 로고    scopus 로고
    • Conjugation of salmon calcitonin to a combed-shaped end functionalized poly(poly(ethylene glycol) methyl ether methacrylate) yields a bioactive stable conjugate
    • Ryan, S. M. et al. Conjugation of salmon calcitonin to a combed-shaped end functionalized poly(poly(ethylene glycol) methyl ether methacrylate) yields a bioactive stable conjugate. J. Control. Release 135, 51-59 (2009).
    • (2009) J. Control. Release , vol.135 , pp. 51-59
    • Ryan, S.M.1
  • 41
    • 26844525474 scopus 로고    scopus 로고
    • Mapping of b-cell epitopes in e. Coli asparaginase ii, an enzyme used in leukemia treatment
    • Werner, A., Röhm, K.-H. & Müller, H.-J. Mapping of B-cell epitopes in E. coli asparaginase II, an enzyme used in leukemia treatment. In: Biol. Chem. 386, 535-540 (2005).
    • (2005) Biol. Chem. , vol.386 , pp. 535-540
    • Werner, A.1    Röhm, K.-H.2    Müller, H.-J.3
  • 42
    • 68849086963 scopus 로고    scopus 로고
    • A dyad of lymphoblastic lysosomal cysteine proteases degrades the antileukemic drug l-Asparaginase
    • Patel, N. et al. A dyad of lymphoblastic lysosomal cysteine proteases degrades the antileukemic drug l-Asparaginase. J. Clin. Invest. 119, 1964-1973 (2009).
    • (2009) J. Clin. Invest. , vol.119 , pp. 1964-1973
    • Patel, N.1
  • 43
    • 33646863688 scopus 로고    scopus 로고
    • Site-specific pegylation of native disulfide bonds in therapeutic proteins
    • Shaunak, S. et al. Site-specific PEGylation of native disulfide bonds in therapeutic proteins. Nat. Chem. Biol. 2, 312-313 (2006).
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 312-313
    • Shaunak, S.1
  • 44
    • 33846406038 scopus 로고    scopus 로고
    • Site-specific pegylation of protein disulfide bonds using a threecarbon bridge
    • Balan, S. et al. Site-specific PEGylation of protein disulfide bonds using a threecarbon bridge. Bioconjug. Chem. 18, 61-76 (2006).
    • (2006) Bioconjug. Chem. , vol.18 , pp. 61-76
    • Balan, S.1
  • 45
    • 84884166196 scopus 로고    scopus 로고
    • Computational design of ligand-binding proteins with high affinity and selectivity
    • Tinberg, C. E. et al. Computational design of ligand-binding proteins with high affinity and selectivity. Nature 501, 212-216 (2013).
    • (2013) Nature , vol.501 , pp. 212-216
    • Tinberg, C.E.1
  • 46
    • 0016073823 scopus 로고
    • Simple and rapid method for estimation of l-Asparaginase in chromatographic and electrophoretic effluents-comparison with other methods
    • Jayaram, H. N., Cooney, D. A., Jayaram, S. & Rosenblu, L. Simple and rapid method for estimation of L-Asparaginase in chromatographic and electrophoretic effluents-comparison with other methods. Anal. Biochem. 59, 327-346 (1974).
    • (1974) Anal. Biochem. , vol.59 , pp. 327-346
    • Jayaram, H.N.1    Cooney, D.A.2    Jayaram, S.3    Rosenblu, L.4
  • 47
    • 0021710691 scopus 로고
    • Rapid analysis of amino-Acids using pre-column derivatization
    • Bidlingmeyer, B. A., Cohen, S. A. & Tarvin, T. L. Rapid analysis of amino-Acids using pre-column derivatization. J. Chromatogr. 336, 93-104 (1984).
    • (1984) J. Chromatogr. , vol.336 , pp. 93-104
    • Bidlingmeyer, B.A.1    Cohen, S.A.2    Tarvin, T.L.3


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