메뉴 건너뛰기




Volumn 152, Issue 3, 2011, Pages 382-392

Tunable elastin-like polypeptide hollow sphere as a high payload and controlled delivery gene depot

Author keywords

Elastin like polypeptide; Hollow sphere and transfection; Monodispersed; Self assembly; Tunable

Indexed keywords

CELL VIABILITY; CONTROLLED DELIVERY; CONTROLLED RELEASE; DIAGNOSTIC APPLICATIONS; ELASTASE; ELASTIN-LIKE POLYPEPTIDES; HOLLOW SPHERE; IN-VITRO; IN-VIVO; LOADING EFFICIENCY; LUCIFERASE EXPRESSION; MICROBIAL TRANSGLUTAMINASE (MTGASE); MONODISPERSED; PLASMID DNA (PDNA); POLYPLEXES; POSITIVE CHARGES; SELF-ASSEMBLED; SURFACE FUNCTIONAL GROUPS; TUNABLE;

EID: 79958242998     PISSN: 01683659     EISSN: 18734995     Source Type: Journal    
DOI: 10.1016/j.jconrel.2011.03.006     Document Type: Article
Times cited : (77)

References (52)
  • 1
    • 77950342360 scopus 로고    scopus 로고
    • Self-assembly of peptide amphiphiles: From molecules to nanostructures to biomaterials
    • H. Cui, M.J. Webber, and S.I. Stupp Self-assembly of peptide amphiphiles: from molecules to nanostructures to biomaterials Biopolymers 94 2010 1 18
    • (2010) Biopolymers , vol.94 , pp. 1-18
    • Cui, H.1    Webber, M.J.2    Stupp, S.I.3
  • 2
    • 70349333526 scopus 로고    scopus 로고
    • Self-assembly and transformation of hybrid nano-objects and nanostructures under equilibrium and non-equilibrium conditions
    • S. Mann Self-assembly and transformation of hybrid nano-objects and nanostructures under equilibrium and non-equilibrium conditions Nat. Mater. 8 2009 781 792
    • (2009) Nat. Mater. , vol.8 , pp. 781-792
    • Mann, S.1
  • 3
    • 34547316314 scopus 로고    scopus 로고
    • Self-assembled peptide nanostructures: The design of molecular building blocks and their technological utilization
    • E. Gazti Self-assembled peptide nanostructures: the design of molecular building blocks and their technological utilization Chem. Soc. Rev. 36 2007 1263 1269
    • (2007) Chem. Soc. Rev. , vol.36 , pp. 1263-1269
    • Gazti, E.1
  • 6
    • 33745268898 scopus 로고    scopus 로고
    • Sustained delivery of plasmid DNA from polymeric scaffolds for tissue engineering
    • DOI 10.1016/j.addr.2006.03.004, PII S0169409X06000524
    • H. Storrie, and D.J. Mooney Sustained delivery of plasmid DNA from polymeric scaffolds for tissue engineering Adv. Drug Deliv. Rev. 58 2006 500 514 (Pubitemid 43928169)
    • (2006) Advanced Drug Delivery Reviews , vol.58 , Issue.4 , pp. 500-514
    • Storrie, H.1    Mooney, D.J.2
  • 7
    • 78649831289 scopus 로고    scopus 로고
    • Recombinant elastin-mimetic biomaterials: Emerging applications in medicine
    • W. Kim, and E.L. Chaikof Recombinant elastin-mimetic biomaterials: emerging applications in medicine Adv. Drug Deliv. Rev. 62 2010 1468 1478
    • (2010) Adv. Drug Deliv. Rev. , vol.62 , pp. 1468-1478
    • Kim, W.1    Chaikof, E.L.2
  • 8
    • 2342424502 scopus 로고    scopus 로고
    • Investigation of recombinant human elastin polypeptides as non-thrombogenic coatings
    • DOI 10.1016/j.biomaterials.2003.11.043, PII S0142961203011086
    • K.A. Woodhouse, P. Klement, V. Chen, M.B. Gorbet, F.W. Keeley, R. Stahl, J.D. Fromstein, and C.M. Bellingham Investigation of recombinant human elastin polypeptides as non-thrombogenic coatings Biomaterials 25 2004 4543 4553 (Pubitemid 38561141)
    • (2004) Biomaterials , vol.25 , Issue.19 , pp. 4543-4553
    • Woodhouse, K.A.1    Klement, P.2    Chen, V.3    Gorbet, M.B.4    Keeley, F.W.5    Stahl, R.6    Fromstein, J.D.7    Bellingham, C.M.8
  • 9
    • 78649884694 scopus 로고    scopus 로고
    • Applications of elastin-like polypeptides in tissue engineering
    • D.L. Nettles, A. Chilkoti, and L.A. Setton Applications of elastin-like polypeptides in tissue engineering Adv. Drug Deliv. Rev. 62 2010 1479 1485
    • (2010) Adv. Drug Deliv. Rev. , vol.62 , pp. 1479-1485
    • Nettles, D.L.1    Chilkoti, A.2    Setton, L.A.3
  • 10
    • 0037130974 scopus 로고    scopus 로고
    • Design of thermally responsive, recombinant polypeptide carriers for targeted drug delivery
    • A. Chilkoti, M.R. Dreher, and D.E. Meyer Design of thermally responsive, recombinant polypeptide carriers for targeted drug delivery Adv. Drug Deliv. Rev. 54 2002 1093 1111
    • (2002) Adv. Drug Deliv. Rev. , vol.54 , pp. 1093-1111
    • Chilkoti, A.1    Dreher, M.R.2    Meyer, D.E.3
  • 11
    • 33751434981 scopus 로고    scopus 로고
    • Stimulus responsive elastin biopolymers: Applications in medicine and biotechnology
    • DOI 10.1016/j.cbpa.2006.10.010, PII S136759310600161X
    • A. Chilkoti, T. Christensen, and J.A. MacKay Stimulus responsive elastin biopolymers: applications in medicine and biotechnology Curr. Opin. Chem. Biol. 10 2006 652 657 (Pubitemid 44821899)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.6 , pp. 652-657
    • Chilkoti, A.1    Christensen, T.2    MacKay, J.A.3
  • 14
    • 34748888993 scopus 로고    scopus 로고
    • Nanobiotechnological approach to engineered biomaterial design: The example of elastin-like polymers
    • J.C. Rodriguez-Cabello, S. Prieto, F.J. Arias, J. Reguera, and A. Ribeiro Nanobiotechnological approach to engineered biomaterial design: the example of elastin-like polymers Nanomedicine 1 2006 267 280
    • (2006) Nanomedicine , vol.1 , pp. 267-280
    • Rodriguez-Cabello, J.C.1    Prieto, S.2    Arias, F.J.3    Reguera, J.4    Ribeiro, A.5
  • 15
    • 17444380093 scopus 로고    scopus 로고
    • Elastin
    • DOI 10.1016/S0065-3233(05)70013-9, Fibrous Proteins Coiled-Coils, Collagen and Elastomers
    • S.M. Mithieux, and A.S. Weiss Elastin Adv. Protein Chem. 70 2005 437 461 (Pubitemid 40544790)
    • (2005) Advances in Protein Chemistry , vol.70 , pp. 437-461
    • Mithieux, S.M.1    Weiss, A.S.2
  • 16
    • 36248980380 scopus 로고    scopus 로고
    • Self-assembled elastin-like polypeptide particles
    • DOI 10.1016/j.actbio.2007.07.007, PII S174270610700116X
    • J.L. Osborne, R. Farmer, and K.A. Woodhouse Self-assembled elastin-like polypeptide particles Acta Biomater. 4 2008 49 57 (Pubitemid 350131557)
    • (2008) Acta Biomaterialia , vol.4 , Issue.1 , pp. 49-57
    • Osborne, J.L.1    Farmer, R.2    Woodhouse, K.A.3
  • 17
    • 0037131001 scopus 로고    scopus 로고
    • Self-assembly of block copolymers derived from elastin-mimetic polypeptide sequences
    • E.R. Wright, and V.P. Conticello Self-assembly of block copolymers derived from elastin-mimetic polypeptide sequences Adv. Drug Deliv. Rev. 54 2002 1057 1073
    • (2002) Adv. Drug Deliv. Rev. , vol.54 , pp. 1057-1073
    • Wright, E.R.1    Conticello, V.P.2
  • 18
    • 0842307664 scopus 로고    scopus 로고
    • Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR
    • DOI 10.1002/mrc.1330
    • X.L. Yao, V.P. Conticello, and M. Hong Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR Magn. Reson. Chem. 42 2004 267 275 (Pubitemid 38178096)
    • (2004) Magnetic Resonance in Chemistry , vol.42 , Issue.2 , pp. 267-275
    • Yao, X.L.1    Conticello, V.P.2    Hong, M.3
  • 19
    • 78650389713 scopus 로고    scopus 로고
    • Quantitative model of the phase behavior of recombinant pH-responsive elastin-like polypeptides
    • J.A. Mackay, D.J. Callahan, K.N. Fitzgerald, and A. Chilkoti Quantitative model of the phase behavior of recombinant pH-responsive elastin-like polypeptides Biomacromolecules 11 2010 2873 2879
    • (2010) Biomacromolecules , vol.11 , pp. 2873-2879
    • MacKay, J.A.1    Callahan, D.J.2    Fitzgerald, K.N.3    Chilkoti, A.4
  • 22
    • 0037185946 scopus 로고    scopus 로고
    • Elastin as a self-organizing biomaterial: Use of recombinantly expressed human elastin polypeptides as a model for investigations of structure and self-assembly of elastin
    • DOI 10.1098/rstb.2001.1027
    • F.W. Keeley, C.M. Bellingham, and K.A. Woodhouse Elastin as a self-organizing biomaterial: use of recombinantly expressed human elastin polypeptides as a model for investigations of structure and self-assembly of elastin Philos. Trans. R. Soc. Lond. B Biol. Sci. 357 2002 185 189 (Pubitemid 34276209)
    • (2002) Philosophical Transactions of the Royal Society B: Biological Sciences , vol.357 , Issue.1418 , pp. 185-189
    • Keeley, F.W.1    Bellingham, C.M.2    Woodhouse, K.A.3
  • 23
    • 77953489827 scopus 로고    scopus 로고
    • Self-assembly of thermally responsive amphiphilic diblock copolypeptides into spherical micellar nanoparticles
    • W. Kim, J. Thevenot, E. Ibarboure, S. Lecommandoux, and E.L. Chaikof Self-assembly of thermally responsive amphiphilic diblock copolypeptides into spherical micellar nanoparticles Angew. Chem. Int. Ed Engl. 49 2010 4257 4260
    • (2010) Angew. Chem. Int. Ed Engl. , vol.49 , pp. 4257-4260
    • Kim, W.1    Thevenot, J.2    Ibarboure, E.3    Lecommandoux, S.4    Chaikof, E.L.5
  • 24
    • 34249829242 scopus 로고    scopus 로고
    • Supramolecular organization of elastin and elastin-related nanostructured biopolymers
    • DOI 10.2217/17435889.2.2.203
    • A. Pepe, B. Bochicchio, and A.M. Tamburro Supramolecular organization of elastin and elastin-related nanostructured biopolymers Nanomedicine (Lond.) 2 2007 203 218 (Pubitemid 46845767)
    • (2007) Nanomedicine , vol.2 , Issue.2 , pp. 203-218
    • Pepe, A.1    Bochicchio, B.2    Tamburro, A.M.3
  • 25
    • 0042697935 scopus 로고    scopus 로고
    • Biopolymers and biomaterials based on elastomeric proteins
    • T. Perri, M. Martino, and A.M. Tamburro Biopolymers and biomaterials based on elastomeric proteins Macromol. Biosci. 2 2002 10
    • (2002) Macromol. Biosci. , vol.2 , pp. 10
    • Perri, T.1    Martino, M.2    Tamburro, A.M.3
  • 26
  • 27
    • 67349269502 scopus 로고    scopus 로고
    • Construction of nanoscale protein particle using temperature-sensitive elastin-like peptide and polyaspartic acid chain
    • Y. Fujita, M. Mie, and E. Kobatake Construction of nanoscale protein particle using temperature-sensitive elastin-like peptide and polyaspartic acid chain Biomaterials 30 2009 3450 3457
    • (2009) Biomaterials , vol.30 , pp. 3450-3457
    • Fujita, Y.1    Mie, M.2    Kobatake, E.3
  • 28
    • 65749117793 scopus 로고    scopus 로고
    • Nanoparticle interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and therapeutic efficacy
    • P. Aggarwal, J.B. Hall, C.B. McLeland, M.A. Dobrovolskaia, and S.E. McNeil Nanoparticle interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and therapeutic efficacy Adv. Drug Deliv. Rev. 61 2009 428 437
    • (2009) Adv. Drug Deliv. Rev. , vol.61 , pp. 428-437
    • Aggarwal, P.1    Hall, J.B.2    McLeland, C.B.3    Dobrovolskaia, M.A.4    McNeil, S.E.5
  • 30
    • 70549101139 scopus 로고    scopus 로고
    • Self-assembling chimeric polypeptide-doxorubicin conjugate nanoparticles that abolish tumours after a single injection
    • J.A. MacKay, M. Chen, J.R. McDaniel, W. Liu, A.J. Simnick, and A. Chilkoti Self-assembling chimeric polypeptide-doxorubicin conjugate nanoparticles that abolish tumours after a single injection Nat. Mater. 8 2009 993 999
    • (2009) Nat. Mater. , vol.8 , pp. 993-999
    • MacKay, J.A.1    Chen, M.2    McDaniel, J.R.3    Liu, W.4    Simnick, A.J.5    Chilkoti, A.6
  • 32
    • 0029608871 scopus 로고
    • Microbial transglutaminase - A review of its production and application in food processing
    • DOI 10.1007/s002530050554
    • Y. Zhu, A. Rinzema, J. Tramper, and J. Bol Microbial transglutaminase-a review of its production and application in food processing Appl. Microbiol. Biotechnol. 44 1995 277 282 (Pubitemid 26024346)
    • (1995) Applied Microbiology and Biotechnology , vol.44 , Issue.3-4 , pp. 277-282
    • Zhu, Y.1    Rinzema, A.2    Tramper, J.3    Bol, J.4
  • 33
    • 33746806632 scopus 로고    scopus 로고
    • Characterization of a microbial transglutaminase cross-linked type II collagen scaffold
    • DOI 10.1089/ten.2006.12.1467
    • D. O'Halloran, R.J. Collighan, M. Griffin, and A.S. Pandit Characterization of a microbial transglutaminase cross-linked type II collagen scaffold Tissue Eng. 12 2006 1467 1474 (Pubitemid 44174782)
    • (2006) Tissue Engineering , vol.12 , Issue.6 , pp. 1467-1474
    • Halloran, D.M.O.1    Collighan, R.J.2    Griffin, M.3    Pandit, A.S.4
  • 34
    • 77649100949 scopus 로고    scopus 로고
    • Use of templates to fabricate nanoscale spherical structures for defined architectural control
    • G. Rethore, and A. Pandit Use of templates to fabricate nanoscale spherical structures for defined architectural control Small 6 2010 488 498
    • (2010) Small , vol.6 , pp. 488-498
    • Rethore, G.1    Pandit, A.2
  • 35
    • 72249113395 scopus 로고    scopus 로고
    • Preparation of chitosan/polyglutamic acid spheres based on the use of polystyrene template as a nonviral gene carrier
    • G. Rethore, A. Mathew, H. Naik, and A. Pandit Preparation of chitosan/polyglutamic acid spheres based on the use of polystyrene template as a nonviral gene carrier Tissue Eng. Part C Methods 15 2009 605 613
    • (2009) Tissue Eng. Part C Methods , vol.15 , pp. 605-613
    • Rethore, G.1    Mathew, A.2    Naik, H.3    Pandit, A.4
  • 36
    • 77956188058 scopus 로고    scopus 로고
    • The influence of size and charge of chitosan/polyglutamic acid hollow spheres on cellular internalization, viability and blood compatibility
    • B.C. Dash, G. Rethore, M. Monaghan, K. Fitzgerald, W. Gallagher, and A. Pandit The influence of size and charge of chitosan/polyglutamic acid hollow spheres on cellular internalization, viability and blood compatibility Biomaterials 31 2010 8188 8197
    • (2010) Biomaterials , vol.31 , pp. 8188-8197
    • Dash, B.C.1    Rethore, G.2    Monaghan, M.3    Fitzgerald, K.4    Gallagher, W.5    Pandit, A.6
  • 37
    • 0032491495 scopus 로고    scopus 로고
    • Nanoengineering of inorganic and hybrid hollow spheres by colloidal templating
    • F. Caruso, R.A. Caruso, and H. Mohwald Nanoengineering of inorganic and hybrid hollow spheres by colloidal templating Science 282 1998 1111 1114 (Pubitemid 28516238)
    • (1998) Science , vol.282 , Issue.5391 , pp. 1111-1114
    • Caruso, F.1    Caruso, R.A.2    Mohwald, H.3
  • 38
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • DOI 10.1016/0003-2697(85)90442-7
    • P.K. Smith, R.I. Krohn, G.T. Hermanson, A.K. Mallia, F.H. Gartner, M.D. Provenzano, E.K. Fujimoto, N.M. Goeke, B.J. Olson, and D.C. Klenk Measurement of protein using bicinchoninic acid Anal. Biochem. 150 1985 76 85 (Pubitemid 16258399)
    • (1985) Analytical Biochemistry , vol.150 , Issue.1 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.T.3
  • 39
    • 0026614994 scopus 로고
    • The determination of epsilon-amino groups in soluble and poorly soluble proteinaceous materials by a spectrophotometric method using trinitrobenzenesulfonic acid
    • W.A. Bubnis, and C.M. Ofner III The determination of epsilon-amino groups in soluble and poorly soluble proteinaceous materials by a spectrophotometric method using trinitrobenzenesulfonic acid Anal. Biochem. 207 1992 129 133
    • (1992) Anal. Biochem. , vol.207 , pp. 129-133
    • Bubnis, W.A.1    Ofner III, C.M.2
  • 40
    • 77953896829 scopus 로고    scopus 로고
    • A highly effective gene delivery vector-hyperbranched poly(2-(dimethylamino)ethyl methacrylate) from in situ deactivation enhanced ATRP
    • B. Newland, H. Tai, Y. Zheng, D. Velasco, A. Di Luca, S.M. Howdle, C. Alexander, W. Wang, and A. Pandit A highly effective gene delivery vector-hyperbranched poly(2-(dimethylamino)ethyl methacrylate) from in situ deactivation enhanced ATRP Chem. Commun. (Camb.) 46 2010 4698 4700
    • (2010) Chem. Commun. (Camb.) , vol.46 , pp. 4698-4700
    • Newland, B.1    Tai, H.2    Zheng, Y.3    Velasco, D.4    Di Luca, A.5    Howdle, S.M.6    Alexander, C.7    Wang, W.8    Pandit, A.9
  • 41
    • 0842325074 scopus 로고    scopus 로고
    • Cationic stearylamine-containing biodegradable microparticles for DNA delivery
    • DOI 10.1080/02652040410001653777
    • C. Kusonwiriyawong, K. Atuah, O.H. Alpar, H.P. Merkle, and E. Walter Cationic stearylamine-containing biodegradable microparticles for DNA delivery J. Microencapsul. 21 2004 25 36 (Pubitemid 38180745)
    • (2004) Journal of Microencapsulation , vol.21 , Issue.1 , pp. 25-36
    • Kusonwiriyawong, C.1    Atuah, K.2    Alphar, O.P.3    Merkle, H.P.4    Walter, E.5
  • 42
    • 0028875936 scopus 로고
    • Transfer of genes to humans: Early lessons and obstacles to success
    • R.G. Crystal Transfer of genes to humans: early lessons and obstacles to success Science 270 1995 404 410
    • (1995) Science , vol.270 , pp. 404-410
    • Crystal, R.G.1
  • 45
    • 0037133097 scopus 로고    scopus 로고
    • PEG grafted polylysine with fusogenic peptide for gene delivery: High transfection efficiency with low cytotoxicity
    • DOI 10.1016/S0168-3659(02)00002-0, PII S0168365902000020
    • H. Lee, J.H. Jeong, and T.G. Park PEG grafted polylysine with fusogenic peptide for gene delivery: high transfection efficiency with low cytotoxicity J. Control. Release 79 2002 283 291 (Pubitemid 34164180)
    • (2002) Journal of Controlled Release , vol.79 , Issue.1-3 , pp. 283-291
    • Lee, H.1    Jeong, J.H.2    Park, T.G.3
  • 46
    • 0026536219 scopus 로고
    • Polyalkylcyanoacrylate nanoparticles as polymeric carriers for antisense oligonucleotides
    • C. Chavany, T. Le Doan, P. Couvreur, F. Puisieux, and C. Helene Polyalkylcyanoacrylate nanoparticles as polymeric carriers for antisense oligonucleotides Pharm. Res. 9 1992 441 449
    • (1992) Pharm. Res. , vol.9 , pp. 441-449
    • Chavany, C.1    Le Doan, T.2    Couvreur, P.3    Puisieux, F.4    Helene, C.5
  • 48
    • 0038004448 scopus 로고    scopus 로고
    • A novel non-viral vector for DNA delivery based on low molecular weight, branched polyethylenimine: Effect of molecular weight on transfection efficiency and cytotoxicity
    • DOI 10.1023/A:1014861900478
    • D. Fischer, T. Bieber, Y. Li, H.P. Elsasser, and T. Kissel A novel non-viral vector for DNA delivery based on low molecular weight, branched polyethylenimine: effect of molecular weight on transfection efficiency and cytotoxicity Pharm. Res. 16 1999 1273 1279 (Pubitemid 29393618)
    • (1999) Pharmaceutical Research , vol.16 , Issue.8 , pp. 1273-1279
    • Fischer, D.1    Bieber, T.2    Li, Y.3    Elsasser, H.-P.4    Kissel, T.5
  • 49
    • 79551617516 scopus 로고    scopus 로고
    • Poly(oligo-D-arginine) with internal disulfide linkages as a cytoplasm-sensitive carrier for siRNA delivery
    • Y.W. Won, S.M. Yoon, K.M. Kim, and Y.H. Lee Poly(oligo-D-arginine) with internal disulfide linkages as a cytoplasm-sensitive carrier for siRNA delivery Mol. Ther. 19 2011 372 380
    • (2011) Mol. Ther. , vol.19 , pp. 372-380
    • Won, Y.W.1    Yoon, S.M.2    Kim, K.M.3    Lee, Y.H.4
  • 50
    • 68949088286 scopus 로고    scopus 로고
    • Dendritic peptide-based carriers for gene delivery
    • I. Toth, and D.J. Coles Dendritic peptide-based carriers for gene delivery Curr. Drug Deliv. 6 2009 338 342
    • (2009) Curr. Drug Deliv. , vol.6 , pp. 338-342
    • Toth, I.1    Coles, D.J.2
  • 51
    • 62849107517 scopus 로고    scopus 로고
    • Cellular uptake of self-assembled cationic peptide-DNA complexes: Multifunctional role of the enhancer chloroquine
    • S. Yang, D.J. Coles, A. Esposito, D.J. Mitchell, I. Toth, and R.F. Minchin Cellular uptake of self-assembled cationic peptide-DNA complexes: multifunctional role of the enhancer chloroquine J. Control. Release 135 2009 159 165
    • (2009) J. Control. Release , vol.135 , pp. 159-165
    • Yang, S.1    Coles, D.J.2    Esposito, A.3    Mitchell, D.J.4    Toth, I.5    Minchin, R.F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.