메뉴 건너뛰기




Volumn 162, Issue 2, 2012, Pages 364-372

In vivo bioactivity of rhBMP-2 delivered with novel polyelectrolyte complexation shells assembled on an alginate microbead core template

Author keywords

Controlled release; Core shell structure; Polyelectrolyte complexes; Recombinant human bone morphogenetic protein 2 (rhBMP 2); Spinal fusion

Indexed keywords

CONTROLLED RELEASE; CORE SHELL STRUCTURE; POLYELECTROLYTE COMPLEXES; RECOMBINANT HUMAN BONE MORPHOGENETIC PROTEIN-2 (RHBMP-2); SPINAL FUSION;

EID: 84865324991     PISSN: 01683659     EISSN: 18734995     Source Type: Journal    
DOI: 10.1016/j.jconrel.2012.07.027     Document Type: Article
Times cited : (47)

References (58)
  • 1
    • 84858112486 scopus 로고    scopus 로고
    • Delivery of dermatan sulfate from polyelectrolyte complex-containing alginate composite microspheres for tissue regeneration
    • Y. Wen, L. Grondahl, M.R. Gallego, L. Jorgensen, E.H. Moller, and H.M. Nielsen Delivery of dermatan sulfate from polyelectrolyte complex-containing alginate composite microspheres for tissue regeneration Biomacromolecules 13 3 2012 905 917
    • (2012) Biomacromolecules , vol.13 , Issue.3 , pp. 905-917
    • Wen, Y.1    Grondahl, L.2    Gallego, M.R.3    Jorgensen, L.4    Moller, E.H.5    Nielsen, H.M.6
  • 3
    • 9644264094 scopus 로고    scopus 로고
    • Encapsulation of biologics in self-assembled fibers as biostructural units for tissue engineering
    • A.C. Wan, E.K. Yim, I.C. Liao, C. Le Visage, and K.W. Leong Encapsulation of biologics in self-assembled fibers as biostructural units for tissue engineering J. Biomed. Mater. Res. A 71 4 2004 586 595
    • (2004) J. Biomed. Mater. Res. A , vol.71 , Issue.4 , pp. 586-595
    • Wan, A.C.1    Yim, E.K.2    Liao, I.C.3    Le Visage, C.4    Leong, K.W.5
  • 4
    • 67049087879 scopus 로고    scopus 로고
    • Polysaccharide-based polyelectrolyte complex nanoparticles from chitosan, heparin, and hyaluronan
    • S. Boddohi, N. Moore, P.A. Johnson, and M.J. Kipper Polysaccharide-based polyelectrolyte complex nanoparticles from chitosan, heparin, and hyaluronan Biomacromolecules 10 6 2009 1402 1409
    • (2009) Biomacromolecules , vol.10 , Issue.6 , pp. 1402-1409
    • Boddohi, S.1    Moore, N.2    Johnson, P.A.3    Kipper, M.J.4
  • 5
    • 66749184130 scopus 로고    scopus 로고
    • Formation and stability of water-soluble, molecular polyelectrolyte complexes: Effects of charge density, mixing ratio, and polyelectrolyte concentration
    • A. Shovsky, I. Varga, R. Makuska, and P.M. Claesson Formation and stability of water-soluble, molecular polyelectrolyte complexes: effects of charge density, mixing ratio, and polyelectrolyte concentration Langmuir 25 11 2009 6113 6121
    • (2009) Langmuir , vol.25 , Issue.11 , pp. 6113-6121
    • Shovsky, A.1    Varga, I.2    Makuska, R.3    Claesson, P.M.4
  • 6
    • 79952993890 scopus 로고    scopus 로고
    • A [polycation:heparin] complex releases growth factors with enhanced bioactivity
    • H. Chu, N.R. Johnson, N.S. Mason, and Y. Wang A [polycation:heparin] complex releases growth factors with enhanced bioactivity J. Control. Release 150 2 2011 157 163
    • (2011) J. Control. Release , vol.150 , Issue.2 , pp. 157-163
    • Chu, H.1    Johnson, N.R.2    Mason, N.S.3    Wang, Y.4
  • 7
    • 80051629333 scopus 로고    scopus 로고
    • Self-assembly of polyamines as a facile approach to fabricate permeability tunable polymeric shells for biomolecular encapsulation
    • J.H. Bai, B. Sebastian, T.S. Yein, and T. Dieter Self-assembly of polyamines as a facile approach to fabricate permeability tunable polymeric shells for biomolecular encapsulation Acs Appl. Mater. Interfaces 3 5 2011 1665 1674
    • (2011) Acs Appl. Mater. Interfaces , vol.3 , Issue.5 , pp. 1665-1674
    • Bai, J.H.1    Sebastian, B.2    Yein, T.S.3    Dieter, T.4
  • 8
    • 33847068324 scopus 로고    scopus 로고
    • Tissue compatibility of interfacial polyelectrolyte complexation fibrous scaffold: Evaluation of blood compatibility and biocompatibility
    • E.K. Yim, I.C. Liao, and K.W. Leong Tissue compatibility of interfacial polyelectrolyte complexation fibrous scaffold: evaluation of blood compatibility and biocompatibility Tissue Eng. 13 2 2007 423 433
    • (2007) Tissue Eng. , vol.13 , Issue.2 , pp. 423-433
    • Yim, E.K.1    Liao, I.C.2    Leong, K.W.3
  • 9
    • 79952758257 scopus 로고    scopus 로고
    • Adsorption characteristics of stoichiometric and nonstoichiometric molecular polyelectrolyte complexes on silicon oxynitride surfaces
    • A. Shovsky, G. Bijelic, I. Varga, R. Makuska, and P.M. Claesson Adsorption characteristics of stoichiometric and nonstoichiometric molecular polyelectrolyte complexes on silicon oxynitride surfaces Langmuir 27 3 2011 1044 1050
    • (2011) Langmuir , vol.27 , Issue.3 , pp. 1044-1050
    • Shovsky, A.1    Bijelic, G.2    Varga, I.3    Makuska, R.4    Claesson, P.M.5
  • 10
    • 0034875812 scopus 로고    scopus 로고
    • New and effective entrapment of polyelectrolyte-enzyme-complexes in LentiKats
    • G. Czichocki, H. Dautzenberg, E. Capan, and K.D. Vorlop New and effective entrapment of polyelectrolyte-enzyme-complexes in LentiKats Biotechnol. Lett. 23 16 2001 1303 1307
    • (2001) Biotechnol. Lett. , vol.23 , Issue.16 , pp. 1303-1307
    • Czichocki, G.1    Dautzenberg, H.2    Capan, E.3    Vorlop, K.D.4
  • 11
    • 0033178916 scopus 로고    scopus 로고
    • Layer-by-layer deposition of oppositely charged polyelectrolytes on the surface of condensed DNA particles
    • V.S. Trubetskoy, A. Loomis, J.E. Hagstrom, V.G. Budker, and J.A. Wolff Layer-by-layer deposition of oppositely charged polyelectrolytes on the surface of condensed DNA particles Nucleic Acids Res. 27 15 1999 3090 3095
    • (1999) Nucleic Acids Res. , vol.27 , Issue.15 , pp. 3090-3095
    • Trubetskoy, V.S.1    Loomis, A.2    Hagstrom, J.E.3    Budker, V.G.4    Wolff, J.A.5
  • 12
    • 10044287286 scopus 로고    scopus 로고
    • An investigation on the physicochemical properties of chitosan/DNA polyelectrolyte complexes
    • W. Liu, S. Sun, Z. Cao, X. Zhang, K. Yao, W.W. Lu, and K.D. Luk An investigation on the physicochemical properties of chitosan/DNA polyelectrolyte complexes Biomaterials 26 15 2005 2705 2711
    • (2005) Biomaterials , vol.26 , Issue.15 , pp. 2705-2711
    • Liu, W.1    Sun, S.2    Cao, Z.3    Zhang, X.4    Yao, K.5    Lu, W.W.6    Luk, K.D.7
  • 13
    • 77956217625 scopus 로고    scopus 로고
    • Control growth factor release using a self-assembled [polycation:heparin] complex
    • B.J. Zern, H. Chu, and Y. Wang Control growth factor release using a self-assembled [polycation:heparin] complex PLoS One 5 6 2010 e11017
    • (2010) PLoS One , vol.5 , Issue.6 , pp. 11017
    • Zern, B.J.1    Chu, H.2    Wang, Y.3
  • 14
    • 80051704822 scopus 로고    scopus 로고
    • Multipoint covalent immobilization of lipase on chitosan hybrid hydrogels: Influence of the polyelectrolyte complex type and chemical modification on the catalytic properties of the biocatalysts
    • A.A. Mendes, H.F. de Castro, S. Rodrigues Dde, W.S. Adriano, P.W. Tardioli, E.J. Mammarella, C. Giordano Rde, and L. Giordano Rde Multipoint covalent immobilization of lipase on chitosan hybrid hydrogels: influence of the polyelectrolyte complex type and chemical modification on the catalytic properties of the biocatalysts J. Ind. Microbiol. Biotechnol. 38 8 2011 1055 1066
    • (2011) J. Ind. Microbiol. Biotechnol. , vol.38 , Issue.8 , pp. 1055-1066
    • Mendes, A.A.1    De Castro, H.F.2    Rodrigues Dde, S.3    Adriano, W.S.4    Tardioli, P.W.5    Mammarella, E.J.6    Giordano Rde, C.7    Giordano Rde, L.8
  • 15
    • 80052554346 scopus 로고    scopus 로고
    • Affinity-based growth factor delivery using biodegradable, photocrosslinked heparin-alginate hydrogels
    • O. Jeon, C. Powell, L.D. Solorio, M.D. Krebs, and E. Alsberg Affinity-based growth factor delivery using biodegradable, photocrosslinked heparin-alginate hydrogels J. Control. Release 154 3 2011 258 266
    • (2011) J. Control. Release , vol.154 , Issue.3 , pp. 258-266
    • Jeon, O.1    Powell, C.2    Solorio, L.D.3    Krebs, M.D.4    Alsberg, E.5
  • 16
    • 0028357322 scopus 로고
    • Stoichiometry of heparin binding to basic fibroblast growth factor
    • T. Arakawa, J. Wen, and J.S. Philo Stoichiometry of heparin binding to basic fibroblast growth factor Arch. Biochem. Biophys. 308 1 1994 267 273
    • (1994) Arch. Biochem. Biophys. , vol.308 , Issue.1 , pp. 267-273
    • Arakawa, T.1    Wen, J.2    Philo, J.S.3
  • 17
    • 0037420913 scopus 로고    scopus 로고
    • Controlling the rate of protein release from polyelectrolyte complexes
    • N. Kamiya, and A.M. Klibanov Controlling the rate of protein release from polyelectrolyte complexes Biotechnol. Bioeng. 82 5 2003 590 594
    • (2003) Biotechnol. Bioeng. , vol.82 , Issue.5 , pp. 590-594
    • Kamiya, N.1    Klibanov, A.M.2
  • 18
    • 79957491846 scopus 로고    scopus 로고
    • The molecular charge and size of heparins determine their impact on the decidualization of human endometrial stromal cells
    • H. Fluhr, J. Spratte, S. Heidrich, J. Ehrhardt, A. Greinacher, and M. Zygmunt The molecular charge and size of heparins determine their impact on the decidualization of human endometrial stromal cells Mol. Hum. Reprod. 17 6 2011 354 359
    • (2011) Mol. Hum. Reprod. , vol.17 , Issue.6 , pp. 354-359
    • Fluhr, H.1    Spratte, J.2    Heidrich, S.3    Ehrhardt, J.4    Greinacher, A.5    Zygmunt, M.6
  • 19
    • 0033525714 scopus 로고    scopus 로고
    • Orientation of heparin-binding sites in native vitronectin. Analyses of ligand binding to the primary glycosaminoglycan-binding site indicate that putative secondary sites are not functional
    • A.D. Gibson, J.A. Lamerdin, P. Zhuang, K. Baburaj, E.H. Serpersu, and C.B. Peterson Orientation of heparin-binding sites in native vitronectin. Analyses of ligand binding to the primary glycosaminoglycan-binding site indicate that putative secondary sites are not functional J. Biol. Chem. 274 10 1999 6432 6442
    • (1999) J. Biol. Chem. , vol.274 , Issue.10 , pp. 6432-6442
    • Gibson, A.D.1    Lamerdin, J.A.2    Zhuang, P.3    Baburaj, K.4    Serpersu, E.H.5    Peterson, C.B.6
  • 20
    • 33847717517 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans (HSPGs) modulate BMP2 osteogenic bioactivity in C2C12 cells
    • X. Jiao, P.C. Billings, M.P. O'Connell, F.S. Kaplan, E.M. Shore, and D.L. Glaser Heparan sulfate proteoglycans (HSPGs) modulate BMP2 osteogenic bioactivity in C2C12 cells J. Biol. Chem. 282 2 2007 1080 1086
    • (2007) J. Biol. Chem. , vol.282 , Issue.2 , pp. 1080-1086
    • Jiao, X.1    Billings, P.C.2    O'Connell, M.P.3    Kaplan, F.S.4    Shore, E.M.5    Glaser, D.L.6
  • 21
    • 0028107098 scopus 로고
    • Structural features in heparin which modulate specific biological activities mediated by basic fibroblast growth factor
    • M. Ishihara, P.N. Shaklee, Z. Yang, W. Liang, Z. Wei, R.J. Stack, and K. Holme Structural features in heparin which modulate specific biological activities mediated by basic fibroblast growth factor Glycobiology 4 4 1994 451 458
    • (1994) Glycobiology , vol.4 , Issue.4 , pp. 451-458
    • Ishihara, M.1    Shaklee, P.N.2    Yang, Z.3    Liang, W.4    Wei, Z.5    Stack, R.J.6    Holme, K.7
  • 22
    • 0036661077 scopus 로고    scopus 로고
    • Interaction of plasminogen activator inhibitor type-1 (PAI-1) with vitronectin (Vn): Mapping the binding sites on PAI-1 and Vn
    • F. Schroeck, N. Arroyo de Prada, S. Sperl, M. Schmitt, and M. Viktor Interaction of plasminogen activator inhibitor type-1 (PAI-1) with vitronectin (Vn): mapping the binding sites on PAI-1 and Vn Biol. Chem. 383 7-8 2002 1143 1149
    • (2002) Biol. Chem. , vol.383 , Issue.78 , pp. 1143-1149
    • Schroeck, F.1    Arroyo De Prada, N.2    Sperl, S.3    Schmitt, M.4    Viktor, M.5
  • 25
    • 0034019945 scopus 로고    scopus 로고
    • Cationic polymer based gene delivery systems
    • S.C. De Smedt, J. Demeester, and W.E. Hennink Cationic polymer based gene delivery systems Pharm. Res. 17 2 2000 113 126
    • (2000) Pharm. Res. , vol.17 , Issue.2 , pp. 113-126
    • De Smedt, S.C.1    Demeester, J.2    Hennink, W.E.3
  • 26
    • 60549096691 scopus 로고    scopus 로고
    • Extracellular matrix stability of primary mammalian chondrocytes and intervertebral disc cells cultured in alginate-based microbead hydrogels
    • S.A. Abbah, W.W. Lu, S.L. Peng, D.M. Aladin, Z.Y. Li, W.K. Tam, K.M. Cheung, K.D. Luk, and G.Q. Zhou Extracellular matrix stability of primary mammalian chondrocytes and intervertebral disc cells cultured in alginate-based microbead hydrogels Cell Transplant. 17 10-11 2008 1181 1192
    • (2008) Cell Transplant. , vol.17 , Issue.1011 , pp. 1181-1192
    • Abbah, S.A.1    Lu, W.W.2    Peng, S.L.3    Aladin, D.M.4    Li, Z.Y.5    Tam, W.K.6    Cheung, K.M.7    Luk, K.D.8    Zhou, G.Q.9
  • 27
    • 80053363820 scopus 로고    scopus 로고
    • Fusion performance of low-dose recombinant human bone morphogenetic protein 2 and bone marrow-derived multipotent stromal cells in biodegradable scaffolds: A comparative study in a large animal model of anterior lumbar interbody fusion
    • (Phila Pa 1976)
    • S.A. Abbah, C.X. Lam, A.K. Ramruttun, J.C. Goh, and H.K. Wong Fusion performance of low-dose recombinant human bone morphogenetic protein 2 and bone marrow-derived multipotent stromal cells in biodegradable scaffolds: a comparative study in a large animal model of anterior lumbar interbody fusion Spine 36 21 2011 1752 1759 (Phila Pa 1976)
    • (2011) Spine , vol.36 , Issue.21 , pp. 1752-1759
    • Abbah, S.A.1    Lam, C.X.2    Ramruttun, A.K.3    Goh, J.C.4    Wong, H.K.5
  • 28
    • 0030130856 scopus 로고    scopus 로고
    • Preparation and surface characterization of functional group-grafted and heparin-immobilized polyurethanes by plasma glow discharge
    • I.K. Kang, O.H. Kwon, Y.M. Lee, and Y.K. Sung Preparation and surface characterization of functional group-grafted and heparin-immobilized polyurethanes by plasma glow discharge Biomaterials 17 8 1996 841 847
    • (1996) Biomaterials , vol.17 , Issue.8 , pp. 841-847
    • Kang, I.K.1    Kwon, O.H.2    Lee, Y.M.3    Sung, Y.K.4
  • 29
    • 70350046442 scopus 로고    scopus 로고
    • Photo-cross-linked hydrogels from thermoresponsive PEGMEMA-PPGMA-EGDMA copolymers containing multiple methacrylate groups: Mechanical property, swelling, protein release, and cytotoxicity
    • H. Tai, D. Howard, S. Takae, W. Wang, T. Vermonden, W.E. Hennink, P.S. Stayton, A.S. Hoffman, A. Endruweit, C. Alexander, S.M. Howdle, and K.M. Shakesheff Photo-cross-linked hydrogels from thermoresponsive PEGMEMA-PPGMA-EGDMA copolymers containing multiple methacrylate groups: mechanical property, swelling, protein release, and cytotoxicity Biomacromolecules 10 10 2009 2895 2903
    • (2009) Biomacromolecules , vol.10 , Issue.10 , pp. 2895-2903
    • Tai, H.1    Howard, D.2    Takae, S.3    Wang, W.4    Vermonden, T.5    Hennink, W.E.6    Stayton, P.S.7    Hoffman, A.S.8    Endruweit, A.9    Alexander, C.10    Howdle, S.M.11    Shakesheff, K.M.12
  • 30
    • 33646769625 scopus 로고    scopus 로고
    • A novel hydroxyapatite fiber mesh as a carrier for recombinant human bone morphogenetic protein-2 enhances bone union in rat posterolateral fusion model
    • (Phila Pa 1976)
    • H. Morisue, M. Matsumoto, K. Chiba, H. Matsumoto, Y. Toyama, M. Aizawa, N. Kanzawa, T.J. Fujimi, H. Uchida, and I. Okada A novel hydroxyapatite fiber mesh as a carrier for recombinant human bone morphogenetic protein-2 enhances bone union in rat posterolateral fusion model Spine 31 11 2006 1194 1200 (Phila Pa 1976)
    • (2006) Spine , vol.31 , Issue.11 , pp. 1194-1200
    • Morisue, H.1    Matsumoto, M.2    Chiba, K.3    Matsumoto, H.4    Toyama, Y.5    Aizawa, M.6    Kanzawa, N.7    Fujimi, T.J.8    Uchida, H.9    Okada, I.10
  • 31
    • 11144279123 scopus 로고    scopus 로고
    • Novel PCL-based honeycomb scaffolds as drug delivery systems for rhBMP-2
    • B. Rai, S.H. Teoh, D.W. Hutmacher, T. Cao, and K.H. Ho Novel PCL-based honeycomb scaffolds as drug delivery systems for rhBMP-2 Biomaterials 26 17 2005 3739 3748
    • (2005) Biomaterials , vol.26 , Issue.17 , pp. 3739-3748
    • Rai, B.1    Teoh, S.H.2    Hutmacher, D.W.3    Cao, T.4    Ho, K.H.5
  • 32
    • 84875886396 scopus 로고    scopus 로고
    • Implant survival analysis and failure modes of the X STOP interspinous distraction device
    • (Phila Pa 1976)
    • A. Tuschel, A. Chavanne, C. Eder, M. Meissl, P. Becker, and M. Ogon Implant survival analysis and failure modes of the X STOP interspinous distraction device Spine 2011 (Phila Pa 1976)
    • (2011) Spine
    • Tuschel, A.1    Chavanne, A.2    Eder, C.3    Meissl, M.4    Becker, P.5    Ogon, M.6
  • 33
    • 78650996715 scopus 로고    scopus 로고
    • Challenges to bone formation in spinal fusion
    • J.J. Reid, J.S. Johnson, and J.C. Wang Challenges to bone formation in spinal fusion J. Biomech. 44 2 2011 213 220
    • (2011) J. Biomech. , vol.44 , Issue.2 , pp. 213-220
    • Reid, J.J.1    Johnson, J.S.2    Wang, J.C.3
  • 34
    • 63649093165 scopus 로고    scopus 로고
    • Rat disc torsional mechanics: Effect of lumbar and caudal levels and axial compression load
    • A.A. Espinoza Orias, N.R. Malhotra, and D.M. Elliott Rat disc torsional mechanics: effect of lumbar and caudal levels and axial compression load Spine J. 9 3 2009 204 209
    • (2009) Spine J. , vol.9 , Issue.3 , pp. 204-209
    • Espinoza Orias, A.A.1    Malhotra, N.R.2    Elliott, D.M.3
  • 35
    • 0027933110 scopus 로고
    • Biomechanical, radiologic, and histopathologic correlations in the pathogenesis of experimental intervertebral disc disease
    • (Phila Pa 1976)
    • B.H. Ziran, S. Pineda, H. Pokharna, A. Esteki, J.M. Mansour, and R.W. Moskowitz Biomechanical, radiologic, and histopathologic correlations in the pathogenesis of experimental intervertebral disc disease Spine 19 19 1994 2159 2163 (Phila Pa 1976)
    • (1994) Spine , vol.19 , Issue.19 , pp. 2159-2163
    • Ziran, B.H.1    Pineda, S.2    Pokharna, H.3    Esteki, A.4    Mansour, J.M.5    Moskowitz, R.W.6
  • 38
    • 0041559960 scopus 로고    scopus 로고
    • Controlled release by biodegradable hydrogels enhances the ectopic bone formation of bone morphogenetic protein
    • M. Yamamoto, Y. Takahashi, and Y. Tabata Controlled release by biodegradable hydrogels enhances the ectopic bone formation of bone morphogenetic protein Biomaterials 24 24 2003 4375 4383
    • (2003) Biomaterials , vol.24 , Issue.24 , pp. 4375-4383
    • Yamamoto, M.1    Takahashi, Y.2    Tabata, Y.3
  • 39
    • 79959555090 scopus 로고    scopus 로고
    • Improving bone formation in a rat femur segmental defect by controlling bone morphogenetic protein-2 release
    • K.V. Brown, B. Li, T. Guda, D.S. Perrien, S.A. Guelcher, and J.C. Wenke Improving bone formation in a rat femur segmental defect by controlling bone morphogenetic protein-2 release Tissue Eng. Part A 17 13-14 2011 1735 1746
    • (2011) Tissue Eng. Part A , vol.17 , Issue.1314 , pp. 1735-1746
    • Brown, K.V.1    Li, B.2    Guda, T.3    Perrien, D.S.4    Guelcher, S.A.5    Wenke, J.C.6
  • 40
    • 0025912560 scopus 로고
    • Extracellular matrix regulation of growth factor and protease activity
    • R. Flaumenhaft, and D.B. Rifkin Extracellular matrix regulation of growth factor and protease activity Curr. Opin. Cell Biol. 3 5 1991 817 823
    • (1991) Curr. Opin. Cell Biol. , vol.3 , Issue.5 , pp. 817-823
    • Flaumenhaft, R.1    Rifkin, D.B.2
  • 41
    • 0026082034 scopus 로고
    • Transforming growth factor beta type 1 binds to collagen IV of basement membrane matrix: Implications for development
    • V.M. Paralkar, S. Vukicevic, and A.H. Reddi Transforming growth factor beta type 1 binds to collagen IV of basement membrane matrix: implications for development Dev. Biol. 143 2 1991 303 308
    • (1991) Dev. Biol. , vol.143 , Issue.2 , pp. 303-308
    • Paralkar, V.M.1    Vukicevic, S.2    Reddi, A.H.3
  • 42
    • 33746928371 scopus 로고    scopus 로고
    • Heparin immobilized porous PLGA microspheres for angiogenic growth factor delivery
    • H.J. Chung, H.K. Kim, J.J. Yoon, and T.G. Park Heparin immobilized porous PLGA microspheres for angiogenic growth factor delivery Pharm. Res. 23 8 2006 1835 1841
    • (2006) Pharm. Res. , vol.23 , Issue.8 , pp. 1835-1841
    • Chung, H.J.1    Kim, H.K.2    Yoon, J.J.3    Park, T.G.4
  • 43
    • 79959831619 scopus 로고    scopus 로고
    • Heparin-decorated, hyaluronic acid-based hydrogel particles for the controlled release of bone morphogenetic protein 2
    • X. Xu, A.K. Jha, R.L. Duncan, and X. Jia Heparin-decorated, hyaluronic acid-based hydrogel particles for the controlled release of bone morphogenetic protein 2 Acta Biomater. 7 8 2011 3050 3059
    • (2011) Acta Biomater. , vol.7 , Issue.8 , pp. 3050-3059
    • Xu, X.1    Jha, A.K.2    Duncan, R.L.3    Jia, X.4
  • 44
    • 9344223942 scopus 로고    scopus 로고
    • Modulation of angiogenic potential of collagen matrices by covalent incorporation of heparin and loading with vascular endothelial growth factor
    • G.C. Steffens, C. Yao, P. Prevel, M. Markowicz, P. Schenck, E.M. Noah, and N. Pallua Modulation of angiogenic potential of collagen matrices by covalent incorporation of heparin and loading with vascular endothelial growth factor Tissue Eng. 10 9-10 2004 1502 1509
    • (2004) Tissue Eng. , vol.10 , Issue.910 , pp. 1502-1509
    • Steffens, G.C.1    Yao, C.2    Prevel, P.3    Markowicz, M.4    Schenck, P.5    Noah, E.M.6    Pallua, N.7
  • 45
    • 77950846241 scopus 로고    scopus 로고
    • Heparin-conjugated fibrin as an injectable system for sustained delivery of bone morphogenetic protein-2
    • H.S. Yang, W.G. La, S.H. Bhang, J.Y. Jeon, J.H. Lee, and B.S. Kim Heparin-conjugated fibrin as an injectable system for sustained delivery of bone morphogenetic protein-2 Tissue Eng. Part A 16 4 2010 1225 1233
    • (2010) Tissue Eng. Part A , vol.16 , Issue.4 , pp. 1225-1233
    • Yang, H.S.1    La, W.G.2    Bhang, S.H.3    Jeon, J.Y.4    Lee, J.H.5    Kim, B.S.6
  • 46
    • 28444474291 scopus 로고    scopus 로고
    • Long-term and zero-order release of basic fibroblast growth factor from heparin-conjugated poly(L-lactide-co-glycolide) nanospheres and fibrin gel
    • O. Jeon, S.W. Kang, H.W. Lim, J. Hyung Chung, and B.S. Kim Long-term and zero-order release of basic fibroblast growth factor from heparin-conjugated poly(L-lactide-co-glycolide) nanospheres and fibrin gel Biomaterials 27 8 2006 1598 1607
    • (2006) Biomaterials , vol.27 , Issue.8 , pp. 1598-1607
    • Jeon, O.1    Kang, S.W.2    Lim, H.W.3    Hyung Chung, J.4    Kim, B.S.5
  • 47
    • 0024508052 scopus 로고
    • Heparin potentiates the action of acidic fibroblast growth factor by prolonging its biological half-life
    • D.H. Damon, R.R. Lobb, P.A. D'Amore, and J.A. Wagner Heparin potentiates the action of acidic fibroblast growth factor by prolonging its biological half-life J. Cell. Physiol. 138 2 1989 221 226
    • (1989) J. Cell. Physiol. , vol.138 , Issue.2 , pp. 221-226
    • Damon, D.H.1    Lobb, R.R.2    D'Amore, P.A.3    Wagner, J.A.4
  • 48
    • 0015866809 scopus 로고
    • Heparin-polypeptide interactions in aqueous solution
    • R.A. Gelman, and J. Blackwell Heparin-polypeptide interactions in aqueous solution Arch. Biochem. Biophys. 159 1 1973 427 433
    • (1973) Arch. Biochem. Biophys. , vol.159 , Issue.1 , pp. 427-433
    • Gelman, R.A.1    Blackwell, J.2
  • 50
    • 0037192290 scopus 로고    scopus 로고
    • Investigation of the influence of polyelectrolyte charge density on the growth of multilayer thin films prepared by the layer-by-layer technique
    • B. Schoeler, G. Kumaraswamy, and F. Caruso Investigation of the influence of polyelectrolyte charge density on the growth of multilayer thin films prepared by the layer-by-layer technique Macromolecules 35 3 2002 889 897
    • (2002) Macromolecules , vol.35 , Issue.3 , pp. 889-897
    • Schoeler, B.1    Kumaraswamy, G.2    Caruso, F.3
  • 51
    • 0037023045 scopus 로고    scopus 로고
    • Influence of charge density and distribution on the internal structure of electrostatically self-assembled polyelectrolyte films
    • M. Koetse, A. Laschewsky, A.M. Jonas, and W. Wagenknecht Influence of charge density and distribution on the internal structure of electrostatically self-assembled polyelectrolyte films Langmuir 18 5 2002 1655 1660
    • (2002) Langmuir , vol.18 , Issue.5 , pp. 1655-1660
    • Koetse, M.1    Laschewsky, A.2    Jonas, A.M.3    Wagenknecht, W.4
  • 52
    • 0028832566 scopus 로고
    • Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin to acidic fibroblast growth factor
    • J.R. Fromm, R.E. Hileman, E.E. Caldwell, J.M. Weiler, and R.J. Linhardt Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin to acidic fibroblast growth factor Arch. Biochem. Biophys. 323 2 1995 279 287
    • (1995) Arch. Biochem. Biophys. , vol.323 , Issue.2 , pp. 279-287
    • Fromm, J.R.1    Hileman, R.E.2    Caldwell, E.E.3    Weiler, J.M.4    Linhardt, R.J.5
  • 53
    • 33846612051 scopus 로고    scopus 로고
    • Continuous polyelectrolyte adsorption under an applied electric potential
    • A.P. Ngankam, and P.R. Van Tassel Continuous polyelectrolyte adsorption under an applied electric potential Proc. Natl. Acad. Sci. U. S. A. 104 4 2007 1140 1145
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , Issue.4 , pp. 1140-1145
    • Ngankam, A.P.1    Van Tassel, P.R.2
  • 54
    • 43349096262 scopus 로고    scopus 로고
    • Complexation of a poly-L-arginine with low molecular weight heparin enhances pulmonary absorption of the drug
    • A. Rawat, T. Yang, A. Hussain, and F. Ahsan Complexation of a poly-L-arginine with low molecular weight heparin enhances pulmonary absorption of the drug Pharm. Res. 25 4 2008 936 948
    • (2008) Pharm. Res. , vol.25 , Issue.4 , pp. 936-948
    • Rawat, A.1    Yang, T.2    Hussain, A.3    Ahsan, F.4
  • 55
    • 2442549670 scopus 로고    scopus 로고
    • Interactions of heparin/heparan sulfate with proteins: Appraisal of structural factors and experimental approaches
    • A.K. Powell, E.A. Yates, D.G. Fernig, and J.E. Turnbull Interactions of heparin/heparan sulfate with proteins: appraisal of structural factors and experimental approaches Glycobiology 14 4 2004 17R 30R
    • (2004) Glycobiology , vol.14 , Issue.4
    • Powell, A.K.1    Yates, E.A.2    Fernig, D.G.3    Turnbull, J.E.4
  • 56
    • 79953041360 scopus 로고    scopus 로고
    • Presentation of BMP-2 from a soft biopolymeric film unveils its activity on cell adhesion and migration
    • T. Crouzier, L. Fourel, T. Boudou, C. Albiges-Rizo, and C. Picart Presentation of BMP-2 from a soft biopolymeric film unveils its activity on cell adhesion and migration Adv. Mater. 23 12 2011 H111 H118
    • (2011) Adv. Mater. , vol.23 , Issue.12
    • Crouzier, T.1    Fourel, L.2    Boudou, T.3    Albiges-Rizo, C.4    Picart, C.5
  • 57
    • 80051962595 scopus 로고    scopus 로고
    • Injectable fibroblast growth factor-2 coacervate for persistent angiogenesis
    • H. Chu, J. Gao, C.W. Chen, J. Huard, and Y. Wang Injectable fibroblast growth factor-2 coacervate for persistent angiogenesis Proc. Natl. Acad. Sci. U. S. A. 108 33 2011 13444 13449
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , Issue.33 , pp. 13444-13449
    • Chu, H.1    Gao, J.2    Chen, C.W.3    Huard, J.4    Wang, Y.5
  • 58
    • 38349056684 scopus 로고    scopus 로고
    • Protein release kinetics for core-shell hybrid nanoparticles based on the layer-by-layer assembly of alginate and chitosan on liposomes
    • Z.S. Haidar, R.C. Hamdy, and M. Tabrizian Protein release kinetics for core-shell hybrid nanoparticles based on the layer-by-layer assembly of alginate and chitosan on liposomes Biomaterials 29 9 2008 1207 1215
    • (2008) Biomaterials , vol.29 , Issue.9 , pp. 1207-1215
    • Haidar, Z.S.1    Hamdy, R.C.2    Tabrizian, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.