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Volumn 97, Issue , 2015, Pages 392-399

From silk spinning in insects and spiders to advanced silk fibroin drug delivery systems

Author keywords

Biomimicry; Crystallization; Drug delivery; Silk fibroin; Spinning

Indexed keywords

ION; SILK; SILK FIBROIN; FIBROIN;

EID: 84948110683     PISSN: 09396411     EISSN: 18733441     Source Type: Journal    
DOI: 10.1016/j.ejpb.2015.03.016     Document Type: Review
Times cited : (19)

References (100)
  • 6
    • 84871538885 scopus 로고    scopus 로고
    • Drug loading and release on tumor cells using silk fibroin-albumin nanoparticles as carriers
    • B. Subia, and S.C. Kundu Drug loading and release on tumor cells using silk fibroin-albumin nanoparticles as carriers Nanotechnology 24 2013 035103
    • (2013) Nanotechnology , vol.24 , pp. 035103
    • Subia, B.1    Kundu, S.C.2
  • 8
    • 77955310355 scopus 로고    scopus 로고
    • Molecular and nanostructural mechanisms of deformation, strength and toughness of spider silk fibrils
    • A. Nova, S. Keten, N.M. Pugno, A. Redaelli, and M.J. Buehler Molecular and nanostructural mechanisms of deformation, strength and toughness of spider silk fibrils Nano Lett. 10 2010 2626 2634
    • (2010) Nano Lett. , vol.10 , pp. 2626-2634
    • Nova, A.1    Keten, S.2    Pugno, N.M.3    Redaelli, A.4    Buehler, M.J.5
  • 9
    • 77955111796 scopus 로고    scopus 로고
    • New opportunities for an ancient material
    • F.G. Omenetto, and D.L. Kaplan New opportunities for an ancient material Science 329 2010 528 531
    • (2010) Science , vol.329 , pp. 528-531
    • Omenetto, F.G.1    Kaplan, D.L.2
  • 10
    • 0002099795 scopus 로고
    • Spiders and their silks
    • F. Lucas Spiders and their silks Discovery 25 1976 20 26
    • (1976) Discovery , vol.25 , pp. 20-26
    • Lucas, F.1
  • 14
    • 70449109302 scopus 로고    scopus 로고
    • Silks as ancient models for modern polymers
    • F. Vollrath, and D. Porter Silks as ancient models for modern polymers Polymer 50 2009 5623 5632
    • (2009) Polymer , vol.50 , pp. 5623-5632
    • Vollrath, F.1    Porter, D.2
  • 15
    • 58449094936 scopus 로고    scopus 로고
    • Silk fibers extruded artificially from aqueous solutions of regenerated Bombyx mori silk fibroin are tougher than their natural counterparts
    • G. Zhou, Z. Shao, D.P. Knight, J. Yan, and X. Chen Silk fibers extruded artificially from aqueous solutions of regenerated Bombyx mori silk fibroin are tougher than their natural counterparts Adv. Mater. 21 2009 366 370
    • (2009) Adv. Mater. , vol.21 , pp. 366-370
    • Zhou, G.1    Shao, Z.2    Knight, D.P.3    Yan, J.4    Chen, X.5
  • 19
    • 84865962769 scopus 로고    scopus 로고
    • Silk fibroin in tissue engineering
    • N. Kasoju, and U. Bora Silk fibroin in tissue engineering Adv. Healthcare Mater. 1 2012 393 412
    • (2012) Adv. Healthcare Mater. , vol.1 , pp. 393-412
    • Kasoju, N.1    Bora, U.2
  • 23
    • 72149093757 scopus 로고    scopus 로고
    • The use of sulfonated silk fibroin derivatives to control binding, delivery and potency of FGF-2 in tissue regeneration
    • E. Wenk, A.R. Murphy, D.L. Kaplan, L. Meinel, H.P. Merkle, and L. Uebersax The use of sulfonated silk fibroin derivatives to control binding, delivery and potency of FGF-2 in tissue regeneration Biomaterials 31 2010 1403 1413
    • (2010) Biomaterials , vol.31 , pp. 1403-1413
    • Wenk, E.1    Murphy, A.R.2    Kaplan, D.L.3    Meinel, L.4    Merkle, H.P.5    Uebersax, L.6
  • 24
    • 60649093062 scopus 로고    scopus 로고
    • Growth factor gradients via microsphere delivery in biopolymer scaffolds for osteochondral tissue engineering
    • X. Wang, E. Wenk, X. Zhang, L. Meinel, G. Vunjak-Novakovic, and D.L. Kaplan Growth factor gradients via microsphere delivery in biopolymer scaffolds for osteochondral tissue engineering J. Control. Release 134 2009 81 90
    • (2009) J. Control. Release , vol.134 , pp. 81-90
    • Wang, X.1    Wenk, E.2    Zhang, X.3    Meinel, L.4    Vunjak-Novakovic, G.5    Kaplan, D.L.6
  • 26
    • 40649088814 scopus 로고    scopus 로고
    • Insulin-like growth factor I releasing silk fibroin scaffolds induce chondrogenic differentiation of human mesenchymal stem cells
    • L. Uebersax, H.P. Merkle, and L. Meinel Insulin-like growth factor I releasing silk fibroin scaffolds induce chondrogenic differentiation of human mesenchymal stem cells J. Control. Release 127 2008 12 21
    • (2008) J. Control. Release , vol.127 , pp. 12-21
    • Uebersax, L.1    Merkle, H.P.2    Meinel, L.3
  • 31
    • 33846133217 scopus 로고    scopus 로고
    • Biocompatibility evaluation of silk fibroin with peripheral nerve tissues and cells in vitro
    • Y. Yang, X. Chen, F. Ding, P. Zhang, J. Liu, and X. Gu Biocompatibility evaluation of silk fibroin with peripheral nerve tissues and cells in vitro Biomaterials 28 2007 1643 1652
    • (2007) Biomaterials , vol.28 , pp. 1643-1652
    • Yang, Y.1    Chen, X.2    Ding, F.3    Zhang, P.4    Liu, J.5    Gu, X.6
  • 33
    • 75949087139 scopus 로고    scopus 로고
    • Cytocompatibility of regenerated silk fibroin film: A medical biomaterial applicable to wound healing
    • T.L. Liu, J.C. Miao, W.H. Sheng, Y.F. Xie, Q. Huang, Y.B. Shan, and J.C. Yang Cytocompatibility of regenerated silk fibroin film: a medical biomaterial applicable to wound healing J. Zhejiang Univ. Sci. B 11 2010 10 16
    • (2010) J. Zhejiang Univ. Sci. B , vol.11 , pp. 10-16
    • Liu, T.L.1    Miao, J.C.2    Sheng, W.H.3    Xie, Y.F.4    Huang, Q.5    Shan, Y.B.6    Yang, J.C.7
  • 36
    • 84858867340 scopus 로고    scopus 로고
    • Review physical and chemical aspects of stabilization of compounds in silk
    • E.M. Pritchard, P.B. Dennis, F. Omenetto, R.R. Naik, and D.L. Kaplan Review physical and chemical aspects of stabilization of compounds in silk Biopolymers 97 2012 479 498
    • (2012) Biopolymers , vol.97 , pp. 479-498
    • Pritchard, E.M.1    Dennis, P.B.2    Omenetto, F.3    Naik, R.R.4    Kaplan, D.L.5
  • 37
    • 0024661113 scopus 로고
    • Immobilization of peroxidase with a Bombyx mori silk fibroin membrane and its application to biophotosensors
    • M. Demura, T. Asakura, E. Nakamura, and H. Tamura Immobilization of peroxidase with a Bombyx mori silk fibroin membrane and its application to biophotosensors J. Biotechnol. 10 1989 113 119
    • (1989) J. Biotechnol. , vol.10 , pp. 113-119
    • Demura, M.1    Asakura, T.2    Nakamura, E.3    Tamura, H.4
  • 38
    • 84865304712 scopus 로고    scopus 로고
    • Silk constructs for delivery of musculoskeletal therapeutics
    • L. Meinel, and D.L. Kaplan Silk constructs for delivery of musculoskeletal therapeutics Adv. Drug Deliv. Rev. 64 2012 1111 1122
    • (2012) Adv. Drug Deliv. Rev. , vol.64 , pp. 1111-1122
    • Meinel, L.1    Kaplan, D.L.2
  • 40
    • 84869084344 scopus 로고    scopus 로고
    • Preparation and in vivo degradation of controlled biodegradability of electrospun silk fibroin nanofiber mats
    • J.H. Kim, C.H. Park, O.J. Lee, J.M. Lee, J.W. Kim, Y.H. Park, and C.S. Ki Preparation and in vivo degradation of controlled biodegradability of electrospun silk fibroin nanofiber mats J. Biomed. Mater. Res. Part A 100 2012 3287 3295
    • (2012) J. Biomed. Mater. Res. Part A , vol.100 , pp. 3287-3295
    • Kim, J.H.1    Park, C.H.2    Lee, O.J.3    Lee, J.M.4    Kim, J.W.5    Park, Y.H.6    Ki, C.S.7
  • 41
    • 60849129103 scopus 로고    scopus 로고
    • Microporous silk fibroin scaffolds embedding PLGA microparticles for controlled growth factor delivery in tissue engineering
    • E. Wenk, A.J. Meinel, S. Wildy, H.P. Merkle, and L. Meinel Microporous silk fibroin scaffolds embedding PLGA microparticles for controlled growth factor delivery in tissue engineering Biomaterials 30 2009 2571 2581
    • (2009) Biomaterials , vol.30 , pp. 2571-2581
    • Wenk, E.1    Meinel, A.J.2    Wildy, S.3    Merkle, H.P.4    Meinel, L.5
  • 42
    • 0037209987 scopus 로고    scopus 로고
    • Enzymatic degradation behavior of porous silk fibroin sheets
    • M. Li, M. Ogiso, and N. Minoura Enzymatic degradation behavior of porous silk fibroin sheets Biomaterials 24 2003 357 365
    • (2003) Biomaterials , vol.24 , pp. 357-365
    • Li, M.1    Ogiso, M.2    Minoura, N.3
  • 43
    • 84891117818 scopus 로고    scopus 로고
    • In vivo biodegradation of porous silk fibroin films implanted beneath the skin and muscle of the rat
    • G. Guan, L. Wang, M. Li, and L. Bai In vivo biodegradation of porous silk fibroin films implanted beneath the skin and muscle of the rat Bio-med. Mater. Eng. 24 2014 789 797
    • (2014) Bio-med. Mater. Eng. , vol.24 , pp. 789-797
    • Guan, G.1    Wang, L.2    Li, M.3    Bai, L.4
  • 44
    • 67149096043 scopus 로고    scopus 로고
    • Biodegradation of silk biomaterials
    • Y. Cao, and B. Wang Biodegradation of silk biomaterials Int. J. Mol. Sci. 10 2009 1514 1524
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 1514-1524
    • Cao, Y.1    Wang, B.2
  • 45
    • 0002312849 scopus 로고
    • Synthesis of silk mechanism and location
    • D.B. Peakall Synthesis of silk mechanism and location Am. Zool. 9 1969 71 79
    • (1969) Am. Zool. , vol.9 , pp. 71-79
    • Peakall, D.B.1
  • 46
    • 0003147034 scopus 로고
    • The amino-acid compositions of major and minor ampullate silks of certain orb-web-building spiders (Araneae, Araneidae)
    • R.W. Work, and C.T. Young The amino-acid compositions of major and minor ampullate silks of certain orb-web-building spiders (Araneae, Araneidae) J. Arachnol. 15 1987 65 80
    • (1987) J. Arachnol. , vol.15 , pp. 65-80
    • Work, R.W.1    Young, C.T.2
  • 47
    • 2542568584 scopus 로고
    • The Nephila clavipes major ampullate gland silk protein, amino acid composition and detection of silk gene-related nucleic acids in the genome
    • S. Lombardi, and D. Kaplan The Nephila clavipes major ampullate gland silk protein, amino acid composition and detection of silk gene-related nucleic acids in the genome Acta Zool. Fennica 190 1991 243
    • (1991) Acta Zool. Fennica , vol.190 , pp. 243
    • Lombardi, S.1    Kaplan, D.2
  • 49
    • 33749443646 scopus 로고
    • The structure and properties of spider silk
    • J.M. Gosline, M.E. DeMont, and M.W. Denny The structure and properties of spider silk Endeavour 10 1986 37 43
    • (1986) Endeavour , vol.10 , pp. 37-43
    • Gosline, J.M.1    DeMont, M.E.2    Denny, M.W.3
  • 50
    • 0017544712 scopus 로고
    • Dimensions, birefringences, and force-elongation behavior of major and minor ampullate silk fibers from orb-web-spinning spiders - Effects of wetting on these properties
    • R.W. Work Dimensions, birefringences, and force-elongation behavior of major and minor ampullate silk fibers from orb-web-spinning spiders - effects of wetting on these properties Text. Res. J. 47 1977 650 662
    • (1977) Text. Res. J. , vol.47 , pp. 650-662
    • Work, R.W.1
  • 51
    • 0042364941 scopus 로고    scopus 로고
    • Mechanism of silk processing in insects and spiders
    • H.-J. Jin, and D.L. Kaplan Mechanism of silk processing in insects and spiders Nature (London, UK) 424 2003 1057 1061
    • (2003) Nature (London, UK) , vol.424 , pp. 1057-1061
    • Jin, H.-J.1    Kaplan, D.L.2
  • 52
    • 84863277914 scopus 로고    scopus 로고
    • Silk self-assembly mechanisms and control from thermodynamics to kinetics
    • Q. Lu, H. Zhu, C. Zhang, F. Zhang, B. Zhang, and D.L. Kaplan Silk self-assembly mechanisms and control from thermodynamics to kinetics Biomacromolecules 13 2012 826 832
    • (2012) Biomacromolecules , vol.13 , pp. 826-832
    • Lu, Q.1    Zhu, H.2    Zhang, C.3    Zhang, F.4    Zhang, B.5    Kaplan, D.L.6
  • 53
    • 9744223571 scopus 로고    scopus 로고
    • Study of protein conformation and orientation in silkworm and spider silk fibers using Raman microspectroscopy
    • M.E. Rousseau, T. Lefevre, L. Beaulieu, T. Asakura, and M. Pezolet Study of protein conformation and orientation in silkworm and spider silk fibers using Raman microspectroscopy Biomacromolecules 5 2004 2247 2257
    • (2004) Biomacromolecules , vol.5 , pp. 2247-2257
    • Rousseau, M.E.1    Lefevre, T.2    Beaulieu, L.3    Asakura, T.4    Pezolet, M.5
  • 54
    • 2542585370 scopus 로고    scopus 로고
    • Spider silk protein refolding is controlled by changing pH
    • C. Dicko, F. Vollrath, and J.M. Kenney Spider silk protein refolding is controlled by changing pH Biomacromolecules 5 2004 704 710
    • (2004) Biomacromolecules , vol.5 , pp. 704-710
    • Dicko, C.1    Vollrath, F.2    Kenney, J.M.3
  • 55
    • 0035967162 scopus 로고    scopus 로고
    • Liquid crystalline spinning of spider silk
    • F. Vollrath, and D.P. Knight Liquid crystalline spinning of spider silk Nature 410 2001 541 548
    • (2001) Nature , vol.410 , pp. 541-548
    • Vollrath, F.1    Knight, D.P.2
  • 56
    • 0034252384 scopus 로고    scopus 로고
    • Strength and structure of spiders' silks
    • F. Vollrath Strength and structure of spiders' silks Rev. Mol. Biotechnol. 74 2000 67 83
    • (2000) Rev. Mol. Biotechnol. , vol.74 , pp. 67-83
    • Vollrath, F.1
  • 57
    • 84881607396 scopus 로고    scopus 로고
    • Morphology and composition of the spider major ampullate gland and dragline silk
    • M. Andersson, L. Holm, Y. Ridderstrale, J. Johansson, and A. Rising Morphology and composition of the spider major ampullate gland and dragline silk Biomacromolecules 14 2013 2945 2952
    • (2013) Biomacromolecules , vol.14 , pp. 2945-2952
    • Andersson, M.1    Holm, L.2    Ridderstrale, Y.3    Johansson, J.4    Rising, A.5
  • 58
    • 0032935646 scopus 로고    scopus 로고
    • Structure and function of the silk production pathway in the spider Nephila edulis
    • F. Vollrath, and D.P. Knight Structure and function of the silk production pathway in the spider Nephila edulis Int. J. Biol. Macromol. 24 1999 243 249
    • (1999) Int. J. Biol. Macromol. , vol.24 , pp. 243-249
    • Vollrath, F.1    Knight, D.P.2
  • 59
    • 33846427680 scopus 로고    scopus 로고
    • Some observations on the structure and function of the spinning apparatus in the silkworm Bombyx mori
    • T. Asakura, K. Umemura, Y. Nakazawa, H. Hirose, J. Higham, and D. Knight Some observations on the structure and function of the spinning apparatus in the silkworm Bombyx mori Biomacromolecules 8 2007 175 181
    • (2007) Biomacromolecules , vol.8 , pp. 175-181
    • Asakura, T.1    Umemura, K.2    Nakazawa, Y.3    Hirose, H.4    Higham, J.5    Knight, D.6
  • 60
    • 8344220569 scopus 로고    scopus 로고
    • Transition to a beta-sheet-rich structure in spidroin in vitro: The effects of pH and cations
    • C. Dicko, J.M. Kenney, D. Knight, and F. Vollrath Transition to a beta-sheet-rich structure in spidroin in vitro: the effects of pH and cations Biochemistry 43 2004 14080 14087
    • (2004) Biochemistry , vol.43 , pp. 14080-14087
    • Dicko, C.1    Kenney, J.M.2    Knight, D.3    Vollrath, F.4
  • 61
    • 80052825015 scopus 로고    scopus 로고
    • Der molekulare Mechanismus der Bildung von Spinnenseide
    • R. Silvers, F. Buhr, and H. Schwalbe Der molekulare Mechanismus der Bildung von Spinnenseide Angew. Chem. 122 2010 5538 5540
    • (2010) Angew. Chem. , vol.122 , pp. 5538-5540
    • Silvers, R.1    Buhr, F.2    Schwalbe, H.3
  • 63
    • 78650693161 scopus 로고    scopus 로고
    • PH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk - Implications for fiber formation
    • F. Hagn, C. Thamm, T. Scheibel, and H. Kessler pH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk - implications for fiber formation Angew. Chem. (Int. Ed. Engl.) 50 2011 310 313
    • (2011) Angew. Chem. (Int. Ed. Engl.) , vol.50 , pp. 310-313
    • Hagn, F.1    Thamm, C.2    Scheibel, T.3    Kessler, H.4
  • 64
    • 84896401674 scopus 로고    scopus 로고
    • Controlled assembly: A prerequisite for the use of recombinant spider silk in regenerative medicine?
    • A. Rising Controlled assembly: a prerequisite for the use of recombinant spider silk in regenerative medicine? Acta Biomater. 10 2014 1627 1631
    • (2014) Acta Biomater. , vol.10 , pp. 1627-1631
    • Rising, A.1
  • 66
    • 84858859727 scopus 로고    scopus 로고
    • Review the role of terminal domains during storage and assembly of spider silk proteins
    • L. Eisoldt, C. Thamm, and T. Scheibel Review the role of terminal domains during storage and assembly of spider silk proteins Biopolymers 97 2012 355 361
    • (2012) Biopolymers , vol.97 , pp. 355-361
    • Eisoldt, L.1    Thamm, C.2    Scheibel, T.3
  • 67
    • 77952378056 scopus 로고    scopus 로고
    • A conserved spider silk domain acts as a molecular switch that controls fibre assembly
    • F. Hagn, L. Eisoldt, J.G. Hardy, C. Vendrely, M. Coles, T. Scheibel, and H. Kessler A conserved spider silk domain acts as a molecular switch that controls fibre assembly Nature 465 2010 239 242
    • (2010) Nature , vol.465 , pp. 239-242
    • Hagn, F.1    Eisoldt, L.2    Hardy, J.G.3    Vendrely, C.4    Coles, M.5    Scheibel, T.6    Kessler, H.7
  • 68
    • 0034978997 scopus 로고    scopus 로고
    • Changes in element composition along the spinning duct in a Nephila spider
    • D.P. Knight, and F. Vollrath Changes in element composition along the spinning duct in a Nephila spider Naturwissenschaften 88 2001 179 182
    • (2001) Naturwissenschaften , vol.88 , pp. 179-182
    • Knight, D.P.1    Vollrath, F.2
  • 70
    • 0033531474 scopus 로고    scopus 로고
    • Liquid crystals and flow elongation in a spider's silk production line
    • D.P. Knight, and F. Vollrath Liquid crystals and flow elongation in a spider's silk production line Proc. R. Soc. B: Biol. Sci. 266 1999 519 523
    • (1999) Proc. R. Soc. B: Biol. Sci. , vol.266 , pp. 519-523
    • Knight, D.P.1    Vollrath, F.2
  • 71
    • 58149375909 scopus 로고    scopus 로고
    • Silk fibroin solution properties related to assembly and structure
    • A. Matsumoto, A. Lindsay, B. Abedian, and D.L. Kaplan Silk fibroin solution properties related to assembly and structure Macromol. Biosci. 8 2008 1006 1018
    • (2008) Macromol. Biosci. , vol.8 , pp. 1006-1018
    • Matsumoto, A.1    Lindsay, A.2    Abedian, B.3    Kaplan, D.L.4
  • 72
    • 2542643108 scopus 로고    scopus 로고
    • PH induced changes in the rheology of silk fibroin solution from the middle division of Bombyx mori silkworm
    • A.E. Terry, D.P. Knight, D. Porter, and F. Vollrath PH induced changes in the rheology of silk fibroin solution from the middle division of Bombyx mori silkworm Biomacromolecules 5 2004 768 772
    • (2004) Biomacromolecules , vol.5 , pp. 768-772
    • Terry, A.E.1    Knight, D.P.2    Porter, D.3    Vollrath, F.4
  • 73
    • 25444514943 scopus 로고    scopus 로고
    • Effect of metallic ions on silk formation in the Mulberry silkworm, Bombyx mori
    • L. Zhou, X. Chen, Z. Shao, Y. Huang, and D.P. Knight Effect of metallic ions on silk formation in the Mulberry silkworm, Bombyx mori J. Phys. Chem. B 109 2005 16937 16945
    • (2005) J. Phys. Chem. B , vol.109 , pp. 16937-16945
    • Zhou, L.1    Chen, X.2    Shao, Z.3    Huang, Y.4    Knight, D.P.5
  • 74
    • 0036859560 scopus 로고    scopus 로고
    • Rheology and dynamic light scattering of silk fibroin solution extracted from the middle division of Bombyx mori silkworm
    • A. Ochi, K.S. Hossain, J. Magoshi, and N. Nemoto Rheology and dynamic light scattering of silk fibroin solution extracted from the middle division of Bombyx mori silkworm Biomacromolecules 3 2002 1187 1196
    • (2002) Biomacromolecules , vol.3 , pp. 1187-1196
    • Ochi, A.1    Hossain, K.S.2    Magoshi, J.3    Nemoto, N.4
  • 75
    • 0034643851 scopus 로고    scopus 로고
    • Beta transition and stress-induced phase separation in the spinning of spider dragline silk
    • D.P. Knight, M.M. Knight, and F. Vollrath Beta transition and stress-induced phase separation in the spinning of spider dragline silk Int. J. Biol. Macromol. 27 2000 205 210
    • (2000) Int. J. Biol. Macromol. , vol.27 , pp. 205-210
    • Knight, D.P.1    Knight, M.M.2    Vollrath, F.3
  • 77
    • 69949145647 scopus 로고    scopus 로고
    • Biopolymer-based growth factor delivery for tissue repair: From natural concepts to engineered systems
    • L. Uebersax, H.P. Merkle, and L. Meinel Biopolymer-based growth factor delivery for tissue repair: from natural concepts to engineered systems Tissue Eng., Part B 15 2009 263 289
    • (2009) Tissue Eng., Part B , vol.15 , pp. 263-289
    • Uebersax, L.1    Merkle, H.P.2    Meinel, L.3
  • 78
    • 84893710225 scopus 로고    scopus 로고
    • Deciphering the mechanism of protein interaction with silk fibroin for drug delivery systems
    • O. Germershaus, V. Werner, M. Kutscher, and L. Meinel Deciphering the mechanism of protein interaction with silk fibroin for drug delivery systems Biomaterials 35 2014 3427 3434
    • (2014) Biomaterials , vol.35 , pp. 3427-3434
    • Germershaus, O.1    Werner, V.2    Kutscher, M.3    Meinel, L.4
  • 79
    • 84871971565 scopus 로고    scopus 로고
    • Self-assembling doxorubicin silk hydrogels for the focal treatment of primary breast cancer
    • F.P. Seib, E.M. Pritchard, and D.L. Kaplan Self-assembling doxorubicin silk hydrogels for the focal treatment of primary breast cancer Adv. Funct. Mater. 23 2013 58 65
    • (2013) Adv. Funct. Mater. , vol.23 , pp. 58-65
    • Seib, F.P.1    Pritchard, E.M.2    Kaplan, D.L.3
  • 81
    • 79955445389 scopus 로고    scopus 로고
    • Mechanisms of controlled release from silk fibroin films
    • D.J. Hines, and D.L. Kaplan Mechanisms of controlled release from silk fibroin films Biomacromolecules 12 2011 804 812
    • (2011) Biomacromolecules , vol.12 , pp. 804-812
    • Hines, D.J.1    Kaplan, D.L.2
  • 82
    • 77954944881 scopus 로고    scopus 로고
    • Silk fibroin-derived nanoparticles for biomedical applications
    • A.B. Mathur, and V. Gupta Silk fibroin-derived nanoparticles for biomedical applications Nanomedicine 5 2010 807 820
    • (2010) Nanomedicine , vol.5 , pp. 807-820
    • Mathur, A.B.1    Gupta, V.2
  • 83
    • 76749124883 scopus 로고    scopus 로고
    • Silk fibroin nanoparticles for cellular uptake and control release
    • J. Kundu, Y.I. Chung, Y.H. Kim, G. Tae, and S.C. Kundu Silk fibroin nanoparticles for cellular uptake and control release Int. J. Pharm. 388 2010 242 250
    • (2010) Int. J. Pharm. , vol.388 , pp. 242-250
    • Kundu, J.1    Chung, Y.I.2    Kim, Y.H.3    Tae, G.4    Kundu, S.C.5
  • 84
    • 84906782250 scopus 로고    scopus 로고
    • Silk-based biomaterials for sustained drug delivery
    • T. Yucel, M.L. Lovett, and D.L. Kaplan Silk-based biomaterials for sustained drug delivery J. Control. Release 190 2014 381 397
    • (2014) J. Control. Release , vol.190 , pp. 381-397
    • Yucel, T.1    Lovett, M.L.2    Kaplan, D.L.3
  • 85
    • 77950682839 scopus 로고    scopus 로고
    • Electrospun scaffolds from silk fibroin and their cellular compatibility
    • K. Zhang, X. Mo, C. Huang, C. He, and H. Wang Electrospun scaffolds from silk fibroin and their cellular compatibility J. Biomed. Mat. Res. Part A 93 2010 976 983
    • (2010) J. Biomed. Mat. Res. Part A , vol.93 , pp. 976-983
    • Zhang, K.1    Mo, X.2    Huang, C.3    He, C.4    Wang, H.5
  • 86
    • 78649819538 scopus 로고    scopus 로고
    • Silk-based delivery systems of bioactive molecules
    • K. Numata, and D.L. Kaplan Silk-based delivery systems of bioactive molecules Adv. Drug Deliv. Rev. 62 2010 1497 1508
    • (2010) Adv. Drug Deliv. Rev. , vol.62 , pp. 1497-1508
    • Numata, K.1    Kaplan, D.L.2
  • 87
    • 84919934092 scopus 로고    scopus 로고
    • Regenerated silk fibroin films with controllable nanostructure size and secondary structure for drug delivery
    • J. Zhou, B. Zhang, L. Shi, J. Zhong, J. Zhu, J. Yan, P. Wang, C. Cao, and D. He Regenerated silk fibroin films with controllable nanostructure size and secondary structure for drug delivery ACS Appl. Mater. Interfaces 6 2014 21813 21821
    • (2014) ACS Appl. Mater. Interfaces , vol.6 , pp. 21813-21821
    • Zhou, J.1    Zhang, B.2    Shi, L.3    Zhong, J.4    Zhu, J.5    Yan, J.6    Wang, P.7    Cao, C.8    He, D.9
  • 89
    • 33646070878 scopus 로고    scopus 로고
    • Regenerated silk fibroin nanofibers: Water vapor-induced structural changes and their effects on the behavior of normal human cells
    • B.-M. Min, L. Jeong, K.Y. Lee, and W.H. Park Regenerated silk fibroin nanofibers: water vapor-induced structural changes and their effects on the behavior of normal human cells Macromol. Biosci. 6 2006 285 292
    • (2006) Macromol. Biosci. , vol.6 , pp. 285-292
    • Min, B.-M.1    Jeong, L.2    Lee, K.Y.3    Park, W.H.4
  • 90
    • 0034023387 scopus 로고    scopus 로고
    • Conformational transitions in model silk peptides
    • D. Wilson, R. Valluzzi, and D. Kaplan Conformational transitions in model silk peptides Biophys. J. 78 2000 2690 2701
    • (2000) Biophys. J. , vol.78 , pp. 2690-2701
    • Wilson, D.1    Valluzzi, R.2    Kaplan, D.3
  • 91
    • 25844435246 scopus 로고    scopus 로고
    • Evidence from 13C solid-state NMR spectroscopy for a lamella structure in an alanine-glycine copolypeptide: A model for the crystalline domain of Bombyx mori silk fiber
    • T. Asakura, Y. Nakazawa, E. Ohnishi, and F. Moro Evidence from 13C solid-state NMR spectroscopy for a lamella structure in an alanine-glycine copolypeptide: a model for the crystalline domain of Bombyx mori silk fiber Protein Sci. 14 2005 2654 2657
    • (2005) Protein Sci. , vol.14 , pp. 2654-2657
    • Asakura, T.1    Nakazawa, Y.2    Ohnishi, E.3    Moro, F.4
  • 93
    • 54949157213 scopus 로고    scopus 로고
    • Silk fibroin spheres as a platform for controlled drug delivery
    • E. Wenk, A.J. Wandrey, H.P. Merkle, and L. Meinel Silk fibroin spheres as a platform for controlled drug delivery J. Control. Release 132 2008 26 34
    • (2008) J. Control. Release , vol.132 , pp. 26-34
    • Wenk, E.1    Wandrey, A.J.2    Merkle, H.P.3    Meinel, L.4
  • 94
    • 84866175348 scopus 로고    scopus 로고
    • Doxorubicin-loaded silk films: Drug-silk interactions and in vivo performance in human orthotopic breast cancer
    • F.P. Seib, and D.L. Kaplan Doxorubicin-loaded silk films: drug-silk interactions and in vivo performance in human orthotopic breast cancer Biomaterials 33 2012 8442 8450
    • (2012) Biomaterials , vol.33 , pp. 8442-8450
    • Seib, F.P.1    Kaplan, D.L.2
  • 97
    • 10044274310 scopus 로고    scopus 로고
    • Three-dimensional aqueous-derived biomaterial scaffolds from silk fibroin
    • U.J. Kim, J. Park, H.J. Kim, M. Wada, and D.L. Kaplan Three-dimensional aqueous-derived biomaterial scaffolds from silk fibroin Biomaterials 26 2005 2775 2785
    • (2005) Biomaterials , vol.26 , pp. 2775-2785
    • Kim, U.J.1    Park, J.2    Kim, H.J.3    Wada, M.4    Kaplan, D.L.5
  • 98
    • 40449126548 scopus 로고    scopus 로고
    • Hydrophobic and Hofmeister effects on the adhesion of spider silk proteins onto solid substrates: An AFM-based single-molecule study
    • M. Geisler, T. Pirzer, C. Ackerschott, S. Lud, J. Garrido, T. Scheibel, and T. Hugel Hydrophobic and Hofmeister effects on the adhesion of spider silk proteins onto solid substrates: an AFM-based single-molecule study Langmuir 24 2008 1350 1355
    • (2008) Langmuir , vol.24 , pp. 1350-1355
    • Geisler, M.1    Pirzer, T.2    Ackerschott, C.3    Lud, S.4    Garrido, J.5    Scheibel, T.6    Hugel, T.7
  • 99
    • 68349139437 scopus 로고    scopus 로고
    • Single molecule force measurements delineate salt, pH and surface effects on biopolymer adhesion
    • T. Pirzer, M. Geisler, T. Scheibel, and T. Hugel Single molecule force measurements delineate salt, pH and surface effects on biopolymer adhesion Phys. Biol. 6 2009 025004
    • (2009) Phys. Biol. , vol.6 , pp. 025004
    • Pirzer, T.1    Geisler, M.2    Scheibel, T.3    Hugel, T.4
  • 100
    • 77951974343 scopus 로고    scopus 로고
    • The role of salt and shear on the storage and assembly of spider silk proteins
    • L. Eisoldt, J.G. Hardy, M. Heim, and T.R. Scheibel The role of salt and shear on the storage and assembly of spider silk proteins J. Struct. Biol. 170 2010 413 419
    • (2010) J. Struct. Biol. , vol.170 , pp. 413-419
    • Eisoldt, L.1    Hardy, J.G.2    Heim, M.3    Scheibel, T.R.4


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