메뉴 건너뛰기




Volumn 183, Issue 1, 2014, Pages 67-76

Cleavable carbamate linkers for controlled protein delivery from hydrogels

Author keywords

Cleavable linker; Hydrogel; Keywords; Poly(ethylene glycol); Protein tethering; Release; Reversible PEGylation

Indexed keywords

CHAINS; CIRCULAR DICHROISM SPECTROSCOPY; ELECTROPHORESIS; ENZYMES; POLYETHYLENE GLYCOLS; PROTEINS; SODIUM DODECYL SULFATE;

EID: 84898024112     PISSN: 01683659     EISSN: 18734995     Source Type: Journal    
DOI: 10.1016/j.jconrel.2014.03.031     Document Type: Article
Times cited : (18)

References (50)
  • 3
    • 34447096637 scopus 로고    scopus 로고
    • Local delivery of proteins and the use of self-assembling peptides
    • DOI 10.1016/j.drudis.2007.05.003, PII S135964460700219X
    • V.F.M. Segers, and R.T. Lee Local delivery of proteins and the use of self-assembling peptides Drug Discov. Today 12 2007 561 568 (Pubitemid 47031660)
    • (2007) Drug Discovery Today , vol.12 , Issue.13-14 , pp. 561-568
    • Segers, V.F.M.1    Lee, R.T.2
  • 4
    • 60149111910 scopus 로고    scopus 로고
    • PEG hydrogels for the controlled release of biomolecules in regenerative medicine
    • C.-C. Lin, and K.S. Anseth PEG hydrogels for the controlled release of biomolecules in regenerative medicine Pharm. Res. 26 2009 631 643
    • (2009) Pharm. Res. , vol.26 , pp. 631-643
    • Lin, C.-C.1    Anseth, K.S.2
  • 5
  • 6
    • 0033818722 scopus 로고    scopus 로고
    • Sustained and controlled release of daunomycin from cross-linked poly(aldehyde guluronate) hydrogels
    • K.H. Bouhadir, G.M. Kruger, K.Y. Lee, and D.J. Mooney Sustained and controlled release of daunomycin from cross-linked poly(aldehyde guluronate) hydrogels J. Pharm. Sci. 89 2000 910 919
    • (2000) J. Pharm. Sci. , vol.89 , pp. 910-919
    • Bouhadir, K.H.1    Kruger, G.M.2    Lee, K.Y.3    Mooney, D.J.4
  • 7
    • 25444497214 scopus 로고    scopus 로고
    • Matrix metalloprotease triggered delivery of cancer chemotherapeutics from hydrogel matrixes
    • DOI 10.1021/bc0501303
    • J.R. Tauro, and R.A. Gemeinhart Matrix metalloprotease triggered delivery of cancer chemotherapeutics from hydrogel matrixes Bioconjug. Chem. 16 2005 1133 1139 (Pubitemid 41368115)
    • (2005) Bioconjugate Chemistry , vol.16 , Issue.5 , pp. 1133-1139
    • Tauro, J.R.1    Gemeinhart, R.A.2
  • 8
    • 0031764072 scopus 로고    scopus 로고
    • Novel degradable poly(ethylene glycol) hydrogels for controlled release of protein
    • X. Zhao, and J. Milton Harris Novel degradable poly(ethylene glycol) hydrogels for controlled release of protein J. Pharm. Sci. 87 1998 1450 1458
    • (1998) J. Pharm. Sci. , vol.87 , pp. 1450-1458
    • Zhao, X.1    Milton Harris, J.2
  • 12
    • 82755160696 scopus 로고    scopus 로고
    • Protein macromonomers containing reduction-sensitive linkers for covalent immobilization and glutathione triggered release from dextran hydrogels
    • E. Verheyen, S. van der Wal, H. Deschout, K. Braeckmans, S. de Smedt, and A. Barendregt et al. Protein macromonomers containing reduction-sensitive linkers for covalent immobilization and glutathione triggered release from dextran hydrogels J. Control. Release 156 2011 329 336
    • (2011) J. Control. Release , vol.156 , pp. 329-336
    • Verheyen, E.1    Van Der Wal, S.2    Deschout, H.3    Braeckmans, K.4    De Smedt, S.5    Barendregt, A.6
  • 13
    • 84873666390 scopus 로고    scopus 로고
    • Diels-Alder mediated controlled release from a poly(ethylene glycol) based hydrogel
    • K.C. Koehler, K.S. Anseth, and C.N. Bowman Diels-Alder mediated controlled release from a poly(ethylene glycol) based hydrogel Biomacromolecules 14 2013 538 547
    • (2013) Biomacromolecules , vol.14 , pp. 538-547
    • Koehler, K.C.1    Anseth, K.S.2    Bowman, C.N.3
  • 14
    • 0037124506 scopus 로고    scopus 로고
    • Chemistry for peptide and protein PEGylation
    • DOI 10.1016/S0169-409X(02)00022-4, PII S0169409X02000224
    • M.J. Roberts, M.D. Bentley, and J.M. Harris Chemistry for peptide and protein PEGylation Adv. Drug Deliv. Rev. 54 2002 459 476 (Pubitemid 34615543)
    • (2002) Advanced Drug Delivery Reviews , vol.54 , Issue.4 , pp. 459-476
    • Roberts, M.J.1    Bentley, M.D.2    Harris, J.M.3
  • 15
    • 0036175670 scopus 로고    scopus 로고
    • Peptide acylation by poly(α-hydroxy esters)
    • DOI 10.1023/A:1014272816454
    • A. Lucke, J. Kiermaier, and A.M. Göpferich Peptide acylation by poly (α-hydroxy esters) Pharm. Res. 19 2002 175 181 (Pubitemid 34165403)
    • (2002) Pharmaceutical Research , vol.19 , Issue.2 , pp. 175-181
    • Lucke, A.1    Kiermaier, J.2    Gopferich, A.3
  • 16
    • 0037161319 scopus 로고    scopus 로고
    • The effect of poly(ethylene glycol)-poly(D,L-lactic acid) diblock copolymers on peptide acylation
    • DOI 10.1016/S0168-3659(02)00020-2, PII S0168365902000202
    • A. Lucke, E. Fustella, J.K. Teßmar, A. Gazzaniga, and A.M. Göpferich The effect of poly (ethylene glycol)-poly (d, l-lactic acid) diblock copolymers on peptide acylation J. Control. Release 80 2002 157 168 (Pubitemid 34273756)
    • (2002) Journal of Controlled Release , vol.80 , Issue.1-3 , pp. 157-168
    • Lucke, A.1    Fustella, E.2    Tessmar, J.3    Gazzaniga, A.4    Gopferich, A.5
  • 17
    • 0035082444 scopus 로고    scopus 로고
    • Drug delivery systems employing 1,6-elimination: Releasable poly(ethylene glycol) conjugates of proteins
    • DOI 10.1021/bc000064z
    • S. Lee, R.B. Greenwald, J. McGuire, K. Yang, and C. Shi Drug delivery systems employing 1,6-elimination: releasable poly(ethylene glycol) conjugates of proteins Bioconjug. Chem. 12 2001 163 169 (Pubitemid 32235467)
    • (2001) Bioconjugate Chemistry , vol.12 , Issue.2 , pp. 163-169
    • Lee, S.1    Greenwald, R.B.2    McGuire, J.3    Yang, K.4    Shi, C.5
  • 18
    • 76249091854 scopus 로고    scopus 로고
    • Biodegradable hydrogels for time-controlled release of tethered peptides or proteins
    • F.P. Brandl, N. Hammer, T. Blunk, J.K. Teßmar, and A.M. Göpferich Biodegradable hydrogels for time-controlled release of tethered peptides or proteins Biomacromolecules 11 2010 496 504
    • (2010) Biomacromolecules , vol.11 , pp. 496-504
    • Brandl, F.P.1    Hammer, N.2    Blunk, T.3    Teßmar, J.K.4    Göpferich, A.M.5
  • 19
    • 0015522277 scopus 로고
    • Fluorescamine: A reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range
    • S. Udenfriend, S. Stein, P. Boehlen, W. Dairman, W. Leimgruber, and M. Weigele Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range Science 178 1972 871 872
    • (1972) Science , vol.178 , pp. 871-872
    • Udenfriend, S.1    Stein, S.2    Boehlen, P.3    Dairman, W.4    Leimgruber, W.5    Weigele, M.6
  • 20
    • 12344336363 scopus 로고    scopus 로고
    • Characterization of site-specific ScFv PEGylation for tumor-targeting pharmaceuticals
    • DOI 10.1021/bc0498121
    • A. Natarajan, C.-Y. Xiong, H. Albrecht, G.L. DeNardo, and S.J. DeNardo Characterization of site-specific ScFv PEGylation for tumor-targeting pharmaceuticals Bioconjug. Chem. 16 2005 113 121 (Pubitemid 40129684)
    • (2005) Bioconjugate Chemistry , vol.16 , Issue.1 , pp. 113-121
    • Natarajan, A.1    Xiong, C.-Y.2    Albrecht, H.3    DeNardo, G.L.4    DeNardo, S.J.5
  • 22
    • 0026530383 scopus 로고
    • Quantitative analysis of protein far UV circular dichroism spectra by neural networks
    • G. Böhm, R. Muhr, and R. Jaenicke Quantitative analysis of protein far UV circular dichroism spectra by neural networks Protein Eng. Des. Sel. 5 1992 191 195
    • (1992) Protein Eng. Des. Sel. , vol.5 , pp. 191-195
    • Böhm, G.1    Muhr, R.2    Jaenicke, R.3
  • 24
    • 34848850746 scopus 로고    scopus 로고
    • An efficient, inexpensive, and shelf-stable diazotransfer reagent: Imidazole-1-sulfonyl azide hydrochloride
    • E.D. Goddard-Borger, and R.V. Stick An efficient, inexpensive, and shelf-stable diazotransfer reagent: imidazole-1-sulfonyl azide hydrochloride Org. Lett. 9 2007 3797 3800
    • (2007) Org. Lett. , vol.9 , pp. 3797-3800
    • Goddard-Borger, E.D.1    Stick, R.V.2
  • 25
    • 34247124903 scopus 로고
    • The measurement of lysozyme activity and the ultra-violet inactivation of lysozyme
    • D. Shugar The measurement of lysozyme activity and the ultra-violet inactivation of lysozyme Biochim. Biophys. Acta 8 1952 302 309
    • (1952) Biochim. Biophys. Acta , vol.8 , pp. 302-309
    • Shugar, D.1
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0033539039 scopus 로고    scopus 로고
    • Drug delivery systems employing 1,4- or 1,6-elimination: Poly(ethylene glycol) prodrugs of amine-containing compounds
    • DOI 10.1021/jm990166e
    • R.B. Greenwald, A. Pendri, C.D. Conover, H. Zhao, Y.H. Choe, and A. Martinez et al. Drug delivery systems employing 1,4- or 1,6-elimination: poly(ethylene glycol) prodrugs of amine-containing compounds J. Med. Chem. 42 1999 3657 3667 (Pubitemid 29445099)
    • (1999) Journal of Medicinal Chemistry , vol.42 , Issue.18 , pp. 3657-3667
    • Greenwald, R.B.1    Pendri, A.2    Conover, C.D.3    Zhao, H.4    Choe, Y.H.5    Martinez, A.6    Shum, K.7    Guan, S.8
  • 28
    • 0037347155 scopus 로고    scopus 로고
    • Controlled release of proteins from their poly(ethylene glycol) conjugates: Drug delivery systems employing 1,6-elimination
    • DOI 10.1021/bc025652m
    • R.B. Greenwald, K. Yang, H. Zhao, C.D. Conover, S. Lee, and D. Filpula Controlled release of proteins from their poly(ethylene glycol) conjugates: drug delivery systems employing 1,6-elimination Bioconjug. Chem. 14 2003 395 403 (Pubitemid 36348663)
    • (2003) Bioconjugate Chemistry , vol.14 , Issue.2 , pp. 395-403
    • Greenwald, R.B.1    Yang, K.2    Zhao, H.3    Conover, C.D.4    Lee, S.5    Filpula, D.6
  • 29
    • 0034628515 scopus 로고    scopus 로고
    • Drug delivery systems based on trimethyl lock lactonization: Poly(ethylene glycol) prodrugs of amino-containing compounds
    • DOI 10.1021/jm990498j
    • R.B. Greenwald, Y.H. Choe, C.D. Conover, K. Shum, D. Wu, and M. Royzen Drug delivery systems based on trimethyl lock lactonization: poly(ethylene glycol) prodrugs of amino-containing compounds J. Med. Chem. 43 2000 475 487 (Pubitemid 30102088)
    • (2000) Journal of Medicinal Chemistry , vol.43 , Issue.3 , pp. 475-487
    • Greenwald, R.B.1    Choe, Y.H.2    Conover, C.D.3    Shum, K.4    Wu, D.5    Royzen, M.6
  • 30
    • 33645469858 scopus 로고    scopus 로고
    • Linear and branched bicin linkers for releasable PEGylation of macromolecules: Controlled release in vivo and in vitro from mono- and multi-PEGylated proteins
    • H. Zhao, K. Yang, A. Martinez, A. Basu, R. Chintala, and H.-C. Liu et al. Linear and branched bicin linkers for releasable PEGylation of macromolecules: Controlled release in vivo and in vitro from mono- and multi-PEGylated proteins Bioconjug. Chem. 17 2006 341 351
    • (2006) Bioconjug. Chem. , vol.17 , pp. 341-351
    • Zhao, H.1    Yang, K.2    Martinez, A.3    Basu, A.4    Chintala, R.5    Liu, H.-C.6
  • 31
    • 0037428969 scopus 로고    scopus 로고
    • Effective drug delivery by PEGylated drug conjugates
    • DOI 10.1016/S0169-409X(02)00180-1, PII S0169409X02001801
    • R.B. Greenwald, Y.H. Choe, J. McGuire, and C.D. Conover Effective drug delivery by PEGylated drug conjugates Adv. Drug Deliv. Rev. 55 2003 217 250 (Pubitemid 36135917)
    • (2003) Advanced Drug Delivery Reviews , vol.55 , Issue.2 , pp. 217-250
    • Greenwald, R.B.1    Choe, Y.H.2    McGuire, J.3    Conover, C.D.4
  • 32
    • 36549050782 scopus 로고    scopus 로고
    • Releasable PEGylation of proteins with customized linkers
    • DOI 10.1016/j.addr.2007.02.001, PII S0169409X07001366, Peptide and Protein PEGylation III: Advances in Chemistry and Clinical Applications
    • D. Filpula, and H. Zhao Releasable PEGylation of proteins with customized linkers Adv. Drug Deliv. Rev. 60 2008 29 49 (Pubitemid 350181165)
    • (2008) Advanced Drug Delivery Reviews , vol.60 , Issue.1 , pp. 29-49
    • Filpula, D.1    Zhao, H.2
  • 33
    • 0000153966 scopus 로고
    • Rates of hydrolysis of carbamate and carbonate esters in alkaline solution
    • L.W. Dittert, and T. Higuchi Rates of hydrolysis of carbamate and carbonate esters in alkaline solution J. Pharm. Sci. 52 1963 852 857
    • (1963) J. Pharm. Sci. , vol.52 , pp. 852-857
    • Dittert, L.W.1    Higuchi, T.2
  • 34
    • 37049142425 scopus 로고
    • Alkaline hydrolysis of substituted phenyl N-phenylcarbamates. Structure-reactivity relationships consistent with an E1cB mechanism
    • A. Williams Alkaline hydrolysis of substituted phenyl N-phenylcarbamates. Structure-reactivity relationships consistent with an E1cB mechanism J. Chem. Soc., Perkin Trans. 2 1972 808 812
    • (1972) J. Chem. Soc., Perkin Trans. 2 , pp. 808-812
    • Williams, A.1
  • 35
    • 37049132783 scopus 로고
    • Elimination-addition mechanism for the hydrolysis of carbamates. Trapping of an isocyanate intermediate by an o-amino-group
    • A.F. Hegarty, and L.N. Frost Elimination-addition mechanism for the hydrolysis of carbamates. Trapping of an isocyanate intermediate by an o-amino-group J. Chem. Soc., Perkin Trans. 2 1973 1719 1728
    • (1973) J. Chem. Soc., Perkin Trans. 2 , pp. 1719-1728
    • Hegarty, A.F.1    Frost, L.N.2
  • 36
    • 0005910343 scopus 로고
    • The question of amide group participation in carbamate hydrolysis
    • A.F. Hegarty, L.N. Frost, and J.H. Coy The question of amide group participation in carbamate hydrolysis J. Org. Chem. 39 1974 1089 1093
    • (1974) J. Org. Chem. , vol.39 , pp. 1089-1093
    • Hegarty, A.F.1    Frost, L.N.2    Coy, J.H.3
  • 37
    • 0026569225 scopus 로고
    • Phenyl carbamates of amino acids as prodrug forms for protecting phenols against first-pass metabolism
    • J. Hansen, N. Mørk, and H. Bundgaard Phenyl carbamates of amino acids as prodrug forms for protecting phenols against first-pass metabolism Int. J. Pharm. 81 1992 253 261
    • (1992) Int. J. Pharm. , vol.81 , pp. 253-261
    • Hansen, J.1    Mørk, N.2    Bundgaard, H.3
  • 38
    • 0031434490 scopus 로고    scopus 로고
    • Influence of quinone methide reactivity on the alkylation of thiol and amino groups in proteins: Studies utilizing amino acid and peptide models
    • DOI 10.1016/S0009-2797(97)00079-3, PII S0009279797000793
    • J.L. Bolton, S.B. Turnipseed, and J.A. Thompson Influence of quinone methide reactivity on the alkylation of thiol and amino groups in proteins: studies utilizing amino acid and peptide models Chem. Biol. Interact. 107 1997 185 200 (Pubitemid 28020547)
    • (1997) Chemico-Biological Interactions , vol.107 , Issue.3 , pp. 185-200
    • Bolton, J.L.1    Turnipseed, S.B.2    Thompson, J.A.3
  • 40
    • 78649832816 scopus 로고    scopus 로고
    • Conjugation of methacrylamide groups to a model protein via a reducible linker for immobilization and subsequent triggered release from hydrogels
    • E. Verheyen, L. Delain-Bioton, S. van der Wal, N. el Morabit, A. Barendregt, and W.E. Hennink et al. Conjugation of methacrylamide groups to a model protein via a reducible linker for immobilization and subsequent triggered release from hydrogels Macromol. Biosci. 10 2010 1517 1526
    • (2010) Macromol. Biosci. , vol.10 , pp. 1517-1526
    • Verheyen, E.1    Delain-Bioton, L.2    Van Der Wal, S.3    El Morabit, N.4    Barendregt, A.5    Hennink, W.E.6
  • 41
    • 0031733869 scopus 로고    scopus 로고
    • Attachment of degradable poly(ethylene glycol) to proteins has the potential to increase therapeutic efficacy
    • M.J. Roberts, and J. Milton Harris Attachment of degradable poly(ethylene glycol) to proteins has the potential to increase therapeutic efficacy J. Pharm. Sci. 87 1998 1440 1445
    • (1998) J. Pharm. Sci. , vol.87 , pp. 1440-1445
    • Roberts, M.J.1    Milton Harris, J.2
  • 42
    • 0033012003 scopus 로고    scopus 로고
    • N-hydroxysuccinimide carbonates and carbamates are useful reactive reagents for coupling ligands to lysines on proteins
    • DOI 10.1016/S0165-022X(98)00027-X, PII S0165022X9800027X
    • M. Morpurgo, E.A. Bayer, and M. Wilchek N-hydroxysuccinimide carbonates and carbamates are useful reactive reagents for coupling ligands to lysines on proteins J. Biochem. Biophys. Methods 38 1999 17 28 (Pubitemid 29050879)
    • (1999) Journal of Biochemical and Biophysical Methods , vol.38 , Issue.1 , pp. 17-28
    • Morpurgo, M.1    Bayer, E.A.2    Wilchek, M.3
  • 43
    • 37049126748 scopus 로고
    • Isocyanate intermediates in E1cb mechanism of carbamate hydrolysis
    • A.F. Hegarty, and L.N. Frost Isocyanate intermediates in E1cb mechanism of carbamate hydrolysis J. Chem. Soc. Chem. Commun. 1972 500 501
    • (1972) J. Chem. Soc. Chem. Commun. , pp. 500-501
    • Hegarty, A.F.1    Frost, L.N.2
  • 44
    • 37049126463 scopus 로고
    • A carbamate anion-isocyanate equilibrium
    • D.J. Woodcock A carbamate anion-isocyanate equilibrium Chem. Commun. (Lond.) 1968 267 268
    • (1968) Chem. Commun. (Lond.) , pp. 267-268
    • Woodcock, D.J.1
  • 45
    • 0023580243 scopus 로고
    • Biochemistry of protein-isocyanate interactions: A comparison of the effects of aryl vs. Alkyl isocyanates
    • W.E. Brown, A.H. Green, T.E. Cedel, and J. Cairns Biochemistry of protein-isocyanate interactions: a comparison of the effects of aryl vs. alkyl isocyanates Environ. Health Perspect. 72 1987 5 11 (Pubitemid 18058043)
    • (1987) Environmental Health Perspectives , vol.72 , pp. 5-11
    • Brown, W.E.1    Green, A.H.2    Cedel, T.E.3    Cairns, J.4
  • 46
    • 0015519012 scopus 로고
    • Conformation of lysozyme in aqueous solution
    • O.G. Hampe Conformation of lysozyme in aqueous solution Eur. J. Biochem. 31 1972 32 37
    • (1972) Eur. J. Biochem. , vol.31 , pp. 32-37
    • Hampe, O.G.1
  • 47
    • 79956205484 scopus 로고    scopus 로고
    • Prevention of benzyl alcohol-induced aggregation of chymotrypsinogen by PEGylation
    • J.A. Rodríguez-Martínez, I. Rivera-Rivera, and K. Griebenow Prevention of benzyl alcohol-induced aggregation of chymotrypsinogen by PEGylation J. Pharm. Pharmacol. 63 2011 800 805
    • (2011) J. Pharm. Pharmacol. , vol.63 , pp. 800-805
    • Rodríguez-Martínez, J.A.1    Rivera-Rivera, I.2    Griebenow, K.3
  • 48
    • 0037735344 scopus 로고    scopus 로고
    • Copper toxicity, oxidative stress, and antioxidant nutrients
    • DOI 10.1016/S0300-483X(03)00159-8
    • L.M. Gaetke, and C.K. Chow Copper toxicity, oxidative stress, and antioxidant nutrients Toxicology 189 2003 147 163 (Pubitemid 36725029)
    • (2003) Toxicology , vol.189 , Issue.1-2 , pp. 147-163
    • Gaetke, L.M.1    Chow, C.K.2
  • 49
    • 81255143206 scopus 로고    scopus 로고
    • Regenerative biomaterials that "click": Simple, aqueous-based protocols for hydrogel synthesis, surface immobilization, and 3D patterning
    • C.M. Nimmo, and M.S. Shoichet Regenerative biomaterials that "click": simple, aqueous-based protocols for hydrogel synthesis, surface immobilization, and 3D patterning Bioconjug. Chem. 22 2011 2199 2209
    • (2011) Bioconjug. Chem. , vol.22 , pp. 2199-2209
    • Nimmo, C.M.1    Shoichet, M.S.2
  • 50
    • 84883311793 scopus 로고    scopus 로고
    • Investigation of the Diels-Alder reaction as a cross-linking mechanism for degradable poly(ethylene glycol) based hydrogels
    • S. Kirchhof, F.P. Brandl, N. Hammer, and A.M. Göpferich Investigation of the Diels-Alder reaction as a cross-linking mechanism for degradable poly(ethylene glycol) based hydrogels J. Mater. Chem. B 1 2013 4855 4864
    • (2013) J. Mater. Chem. B , vol.1 , pp. 4855-4864
    • Kirchhof, S.1    Brandl, F.P.2    Hammer, N.3    Göpferich, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.