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Volumn 119, Issue 3, 2007, Pages 301-312

Recombinant gelatin hydrogels for the sustained release of proteins

Author keywords

Diffusion; Hydrogels; Protein delivery; Recombinant gelatin; Sustained release

Indexed keywords

AMINO ACIDS; BIODEGRADABILITY; CROSSLINKING; FREE RADICAL POLYMERIZATION; PHYSIOLOGY; POLYMERS; PROTEINS;

EID: 34249098497     PISSN: 01683659     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jconrel.2007.03.003     Document Type: Article
Times cited : (114)

References (58)
  • 1
    • 0034997401 scopus 로고    scopus 로고
    • Development and characterization of a novel erythropoiesis stimulating protein (nesp)
    • Egrie J.C., and Brown J.K. Development and characterization of a novel erythropoiesis stimulating protein (nesp). Br. J. Cancer 84 Supplement 1 (2001) 3-10
    • (2001) Br. J. Cancer , vol.84 , Issue.SUPPL. 1 , pp. 3-10
    • Egrie, J.C.1    Brown, J.K.2
  • 3
    • 3843142857 scopus 로고    scopus 로고
    • Second-generation biopharmaceuticals
    • Walsh G. Second-generation biopharmaceuticals. Eur. J. Pharm. Biopharm. 58 (2004) 185-196
    • (2004) Eur. J. Pharm. Biopharm. , vol.58 , pp. 185-196
    • Walsh, G.1
  • 4
    • 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 Supplement 6 (2005) 3-9
    • (2005) Nephrol. Dial. Transplant. , vol.20 , Issue.SUPPL. 6 , pp. 3-9
    • Schellekens, H.1
  • 6
    • 0031766727 scopus 로고    scopus 로고
    • The structure of human interferon-β: implications for activity
    • Karpusas M., Whitty A., Runkel L., and Hochman P. The structure of human interferon-β: implications for activity. Cell. Mol. Life Sci. 54 (1998) 1203-1216
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 1203-1216
    • Karpusas, M.1    Whitty, A.2    Runkel, L.3    Hochman, P.4
  • 8
    • 0037122788 scopus 로고    scopus 로고
    • Novel crosslinking methods to design hydrogels
    • Hennink W.E., and van Nostrum C.F. Novel crosslinking methods to design hydrogels. Adv. Drug Deliv. Rev. 54 (2002) 13-36
    • (2002) Adv. Drug Deliv. Rev. , vol.54 , pp. 13-36
    • Hennink, W.E.1    van Nostrum, C.F.2
  • 10
    • 0038445582 scopus 로고    scopus 로고
    • Biodegradable microspheres for protein delivery
    • Sinha V.R., and Trehan A. Biodegradable microspheres for protein delivery. J. Control. Release 90 (2003) 261-280
    • (2003) J. Control. Release , vol.90 , pp. 261-280
    • Sinha, V.R.1    Trehan, A.2
  • 11
    • 0029335538 scopus 로고
    • Biodegradable polymers for protein and peptide drug delivery
    • Gombotz W.R., and Pettit D.K. Biodegradable polymers for protein and peptide drug delivery. Bioconjug. Chem. 6 (1995) 332-351
    • (1995) Bioconjug. Chem. , vol.6 , pp. 332-351
    • Gombotz, W.R.1    Pettit, D.K.2
  • 14
    • 0035962384 scopus 로고    scopus 로고
    • Physically crosslinked dextran hydrogels by stereocomplex formation of lactic acid oligomers: degradation and protein release behavior
    • de Jong S.J., van Eerdenbrugh B., van Nostrum C.F., Kettenes-van den Bosch J.J., and Hennink W.E. Physically crosslinked dextran hydrogels by stereocomplex formation of lactic acid oligomers: degradation and protein release behavior. J. Control. Release 71 (2001) 261-275
    • (2001) J. Control. Release , vol.71 , pp. 261-275
    • de Jong, S.J.1    van Eerdenbrugh, B.2    van Nostrum, C.F.3    Kettenes-van den Bosch, J.J.4    Hennink, W.E.5
  • 16
    • 0030444591 scopus 로고    scopus 로고
    • Biocompatibility issues of implantable drug delivery systems
    • Park H., and Park K. Biocompatibility issues of implantable drug delivery systems. Pharm. Res. 13 (1996) 1770-1776
    • (1996) Pharm. Res. , vol.13 , pp. 1770-1776
    • Park, H.1    Park, K.2
  • 18
    • 0032482156 scopus 로고    scopus 로고
    • Protein release from gelatin matrices
    • Tabata Y., and Ikida Y. Protein release from gelatin matrices. Adv. Drug Deliv. Rev. 31 (1998) 287-301
    • (1998) Adv. Drug Deliv. Rev. , vol.31 , pp. 287-301
    • Tabata, Y.1    Ikida, Y.2
  • 22
    • 0242710145 scopus 로고    scopus 로고
    • Collagens - structure, function, and biosynthesis
    • Gelse K., Pöschl E., and Aigner T. Collagens - structure, function, and biosynthesis. Adv. Drug Deliv. Rev. 55 (2003) 1531-1546
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 1531-1546
    • Gelse, K.1    Pöschl, E.2    Aigner, T.3
  • 23
    • 33747199346 scopus 로고    scopus 로고
    • Static light scattering and small-angle neutron scattering study on aggregated recombinant gelatin in aqueous solution
    • Ramzi A., Sutter M., Hennink W.E., and Jiskoot W. Static light scattering and small-angle neutron scattering study on aggregated recombinant gelatin in aqueous solution. J. Pharm. Sci. 95 (2006) 1703-1711
    • (2006) J. Pharm. Sci. , vol.95 , pp. 1703-1711
    • Ramzi, A.1    Sutter, M.2    Hennink, W.E.3    Jiskoot, W.4
  • 24
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace C.N., Vajdos F., Fee L., Grimsley G., and Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4 (1995) 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 25
    • 0346663046 scopus 로고    scopus 로고
    • Effects of polysaccharides on the stability and renaturation of soybean trypsin (kunitz) inhibitor
    • Burova T.V., Varfolomeeva E.P., Grinberg V.A., Haertle T., and Tolstoguzov V.B. Effects of polysaccharides on the stability and renaturation of soybean trypsin (kunitz) inhibitor. Macromol. Biosci. 2 (2002) 286-292
    • (2002) Macromol. Biosci. , vol.2 , pp. 286-292
    • Burova, T.V.1    Varfolomeeva, E.P.2    Grinberg, V.A.3    Haertle, T.4    Tolstoguzov, V.B.5
  • 27
    • 0022999267 scopus 로고
    • Compressibiltiy-structure relationship of globular proteins
    • Gekko K., and Hasegawa Y. Compressibiltiy-structure relationship of globular proteins. Biochemistry 25 (1986) 6563-6571
    • (1986) Biochemistry , vol.25 , pp. 6563-6571
    • Gekko, K.1    Hasegawa, Y.2
  • 28
    • 0037026274 scopus 로고    scopus 로고
    • A comparison between the use of dynamic mechanical analysis and oscillatory shear rheometry for the characterisation of hydrogels
    • Meyvis T.K.L., Stubbe B.G., van Steenbergen M.J., Hennink W.E., De Smedt S.C., and Demeester J. A comparison between the use of dynamic mechanical analysis and oscillatory shear rheometry for the characterisation of hydrogels. Int. J. Pharm. 244 (2002) 163-168
    • (2002) Int. J. Pharm. , vol.244 , pp. 163-168
    • Meyvis, T.K.L.1    Stubbe, B.G.2    van Steenbergen, M.J.3    Hennink, W.E.4    De Smedt, S.C.5    Demeester, J.6
  • 29
    • 34248349905 scopus 로고    scopus 로고
    • Viscoelasticity and flow in polymeric liquids
    • Mark J.E., Ngai K.L., Graessly W.W., Mandelkern L., Samulski E.T., Koenig J.L., and Wignall G.D. (Eds), Cambridge University Press, Cambridge
    • Graessly W.W. Viscoelasticity and flow in polymeric liquids. In: Mark J.E., Ngai K.L., Graessly W.W., Mandelkern L., Samulski E.T., Koenig J.L., and Wignall G.D. (Eds). Physical Properties of Polymers, (2004), Cambridge University Press, Cambridge 153-208
    • (2004) Physical Properties of Polymers , pp. 153-208
    • Graessly, W.W.1
  • 31
    • 2942551376 scopus 로고    scopus 로고
    • Crosslinked gelatin matrices: release of a random coil macromolecular solute
    • Mwangi J.W., and Ofner C.M. Crosslinked gelatin matrices: release of a random coil macromolecular solute. Int. J. Pharm. 278 (2004) 319-327
    • (2004) Int. J. Pharm. , vol.278 , pp. 319-327
    • Mwangi, J.W.1    Ofner, C.M.2
  • 33
    • 0031455780 scopus 로고    scopus 로고
    • Biological activity of lysozyme after entrapment in poly(d,l-lactide-co-glycolyde)-microspheres
    • Ghaderi R., and Calfors J. Biological activity of lysozyme after entrapment in poly(d,l-lactide-co-glycolyde)-microspheres. Pharm. Res. 14 (1997) 1556-1562
    • (1997) Pharm. Res. , vol.14 , pp. 1556-1562
    • Ghaderi, R.1    Calfors, J.2
  • 34
    • 0031825269 scopus 로고    scopus 로고
    • Calculation of the dimensions of drug-polymer devices based on diffusion parameters
    • Siepmann J., Ainaoui A., Vergnaud J.M., and Bodmeier R. Calculation of the dimensions of drug-polymer devices based on diffusion parameters. J. Pharm. Sci. 87 (1998) 827-832
    • (1998) J. Pharm. Sci. , vol.87 , pp. 827-832
    • Siepmann, J.1    Ainaoui, A.2    Vergnaud, J.M.3    Bodmeier, R.4
  • 35
    • 0026795140 scopus 로고
    • Matrix metalloproteinase 9 (92-kDa gelatinase/type iv collagenase) from ht1080 human fibrosarcoma cells
    • Okada Y., Gonoji Y., Naka K., Tomita K., Nakanishi I., Iwata K., Yamashita K., and Hayakawa T. Matrix metalloproteinase 9 (92-kDa gelatinase/type iv collagenase) from ht1080 human fibrosarcoma cells. J. Biol. Chem. 267 (1992) 21712-21719
    • (1992) J. Biol. Chem. , vol.267 , pp. 21712-21719
    • Okada, Y.1    Gonoji, Y.2    Naka, K.3    Tomita, K.4    Nakanishi, I.5    Iwata, K.6    Yamashita, K.7    Hayakawa, T.8
  • 37
    • 0015080147 scopus 로고
    • Characterization of collagen peptides by sodium dodecylsulfate-polyacrylamide electrophoresis
    • Furthmayr H., and Timpl R. Characterization of collagen peptides by sodium dodecylsulfate-polyacrylamide electrophoresis. Anal. Biochem. 41 (1971) 510-516
    • (1971) Anal. Biochem. , vol.41 , pp. 510-516
    • Furthmayr, H.1    Timpl, R.2
  • 39
    • 0017384070 scopus 로고
    • Resistance of soybean trypsin inhibitor (kunitz) to denaturation by guanidinium chloride
    • Leach B.S., and Fish W.W. Resistance of soybean trypsin inhibitor (kunitz) to denaturation by guanidinium chloride. J. Biol. Chem. 252 (1977) 5239-5243
    • (1977) J. Biol. Chem. , vol.252 , pp. 5239-5243
    • Leach, B.S.1    Fish, W.W.2
  • 40
    • 20744455838 scopus 로고    scopus 로고
    • Hydrodynamic radius ladders of proteins
    • Sharma U., and Carbeck J.D. Hydrodynamic radius ladders of proteins. Electrophoresis 26 (2005) 2086-2091
    • (2005) Electrophoresis , vol.26 , pp. 2086-2091
    • Sharma, U.1    Carbeck, J.D.2
  • 41
    • 33751195735 scopus 로고    scopus 로고
    • Hydrogels in controlled release formulations: network design and mathematical modeling
    • Lin C.C., and Metters A.T. Hydrogels in controlled release formulations: network design and mathematical modeling. Adv. Drug Deliv. Rev. 58 (2006) 1379-1408
    • (2006) Adv. Drug Deliv. Rev. , vol.58 , pp. 1379-1408
    • Lin, C.C.1    Metters, A.T.2
  • 42
    • 0033742086 scopus 로고    scopus 로고
    • 2 solutions from dynamic light-scattering data: effect of protein and salt concentrations
    • 2 solutions from dynamic light-scattering data: effect of protein and salt concentrations. J. Phys. Chem., B 104 (2000) 3645-3650
    • (2000) J. Phys. Chem., B , vol.104 , pp. 3645-3650
    • Grigsby, J.J.1    Blanch, H.W.2    Prausnitz, J.M.3
  • 43
    • 0020840829 scopus 로고
    • Solute diffusion in swollen membranes. Part i. A new theory
    • Peppas N.A., and Reinhart C.T. Solute diffusion in swollen membranes. Part i. A new theory. J. Membr. Sci. 15 (1983) 275-287
    • (1983) J. Membr. Sci. , vol.15 , pp. 275-287
    • Peppas, N.A.1    Reinhart, C.T.2
  • 45
    • 0028949146 scopus 로고
    • Diffusion and partitioning of proteins in charged agarose gels
    • Johnson E.M., Berk D.A., Jain R.K., and Deen W.M. Diffusion and partitioning of proteins in charged agarose gels. Biophys. J. 68 (1995) 1561-1568
    • (1995) Biophys. J. , vol.68 , pp. 1561-1568
    • Johnson, E.M.1    Berk, D.A.2    Jain, R.K.3    Deen, W.M.4
  • 47
    • 0005127283 scopus 로고    scopus 로고
    • Ionic strength dependence of protein adsorption to dye-ligand adsorbents
    • Zhang S., and Sun Y. Ionic strength dependence of protein adsorption to dye-ligand adsorbents. AIChE J. 48 (2002) 178-186
    • (2002) AIChE J. , vol.48 , pp. 178-186
    • Zhang, S.1    Sun, Y.2
  • 48
    • 0000795707 scopus 로고
    • Isolation of a crystalline protein compound of trypsin and of soybean trypsin-inhibitor
    • Kunitz M. Isolation of a crystalline protein compound of trypsin and of soybean trypsin-inhibitor. J. Gen. Physiol. 30 (1947) 311-320
    • (1947) J. Gen. Physiol. , vol.30 , pp. 311-320
    • Kunitz, M.1
  • 50
    • 0035051778 scopus 로고    scopus 로고
    • Controlled release of growth factors based on biodegradation of gelatin hydrogel
    • Yamamoto M., Ikada Y., and Tabata Y. Controlled release of growth factors based on biodegradation of gelatin hydrogel. J. Biomater. Sci., Polym. Ed. 12 (2001) 77-88
    • (2001) J. Biomater. Sci., Polym. Ed. , vol.12 , pp. 77-88
    • Yamamoto, M.1    Ikada, Y.2    Tabata, Y.3
  • 54
    • 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
  • 57
    • 15244343155 scopus 로고    scopus 로고
    • In vivo evaluation of poly(n-isopropylacrylamide) (pnipam)-grafted gelatin as an in-situ formable scaffold
    • Ohya S., and Nakayama Y. In vivo evaluation of poly(n-isopropylacrylamide) (pnipam)-grafted gelatin as an in-situ formable scaffold. J. Artif. Organs 7 (2004) 181-186
    • (2004) J. Artif. Organs , vol.7 , pp. 181-186
    • Ohya, S.1    Nakayama, Y.2
  • 58
    • 0036242269 scopus 로고    scopus 로고
    • Thermoresponsive artificial extracellular matrix: N-isopropylacrylamide-graft-copolymerized gelatin
    • Morikawa N., and Matsuda T. Thermoresponsive artificial extracellular matrix: N-isopropylacrylamide-graft-copolymerized gelatin. J. Biomater. Sci., Polym. Ed. 13 (2002) 167-183
    • (2002) J. Biomater. Sci., Polym. Ed. , vol.13 , pp. 167-183
    • Morikawa, N.1    Matsuda, T.2


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