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Volumn 7, Issue 11, 2012, Pages

Recombinant Minimalist Spider Wrapping Silk Proteins Capable of Native-Like Fiber Formation

Author keywords

[No Author keywords available]

Indexed keywords

ACINIFORM PROTEIN 1; ESCHERICHIA COLI PROTEIN; INSECT PROTEIN; RECOMBINANT PROTEIN; SILK; SPIDER WRAPPING SILK; UNCLASSIFIED DRUG;

EID: 84870347032     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0050227     Document Type: Article
Times cited : (67)

References (34)
  • 1
    • 70350700449 scopus 로고    scopus 로고
    • Animal silks: their structures, properties and artificial production
    • Fu C, Shao Z, Fritz V (2009) Animal silks: their structures, properties and artificial production. Chem Commun (Camb): 6515-6529.
    • (2009) Chem Commun (Camb) , pp. 6515-6529
    • Fu, C.1    Shao, Z.2    Fritz, V.3
  • 2
    • 33845332079 scopus 로고    scopus 로고
    • Use of spider silk fibres as an innovative material in a biocompatible artificial nerve conduit
    • Allmeling C, Jokuszies A, Reimers K, Kall S, Vogt PM, (2006) Use of spider silk fibres as an innovative material in a biocompatible artificial nerve conduit. J Cell Mol Med 10: 770-777.
    • (2006) J Cell Mol Med , vol.10 , pp. 770-777
    • Allmeling, C.1    Jokuszies, A.2    Reimers, K.3    Kall, S.4    Vogt, P.M.5
  • 3
    • 79960825396 scopus 로고    scopus 로고
    • Artificial skin-culturing of different skin cell lines for generating an artificial skin substitute on cross-weaved spider silk fibres
    • Wendt H, Hillmer A, Reimers K, Kuhbier JW, Schafer-Nolte F, et al. (2011) Artificial skin-culturing of different skin cell lines for generating an artificial skin substitute on cross-weaved spider silk fibres. PLoS One 6: e21833.
    • (2011) PLoS One , vol.6
    • Wendt, H.1    Hillmer, A.2    Reimers, K.3    Kuhbier, J.W.4    Schafer-Nolte, F.5
  • 4
    • 84858865571 scopus 로고    scopus 로고
    • Invited review current progress and limitations of spider silk for biomedical applications
    • Widhe M, Johansson J, Hedhammar M, Rising A, (2012) Invited review current progress and limitations of spider silk for biomedical applications. Biopolymers 97: 468-478.
    • (2012) Biopolymers , vol.97 , pp. 468-478
    • Widhe, M.1    Johansson, J.2    Hedhammar, M.3    Rising, A.4
  • 5
    • 77956296603 scopus 로고    scopus 로고
    • Native-sized recombinant spider silk protein produced in metabolically engineered Escherichia coli results in a strong fiber
    • Xia XX, Qian ZG, Ki CS, Park YH, Kaplan DL, et al. (2010) Native-sized recombinant spider silk protein produced in metabolically engineered Escherichia coli results in a strong fiber. Proc Natl Acad Sci U S A 107: 14059-14063.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 14059-14063
    • Xia, X.X.1    Qian, Z.G.2    Ki, C.S.3    Park, Y.H.4    Kaplan, D.L.5
  • 6
    • 33847121737 scopus 로고    scopus 로고
    • Construct synthetic gene encoding artificial spider dragline silk protein and its expression in milk of transgenic mice
    • Xu HT, Fan BL, Yu SY, Huang YH, Zhao ZH, et al. (2007) Construct synthetic gene encoding artificial spider dragline silk protein and its expression in milk of transgenic mice. Anim Biotechnol 18: 1-12.
    • (2007) Anim Biotechnol , vol.18 , pp. 1-12
    • Xu, H.T.1    Fan, B.L.2    Yu, S.Y.3    Huang, Y.H.4    Zhao, Z.H.5
  • 7
    • 0031051471 scopus 로고    scopus 로고
    • Production of synthetic spider dragline silk protein in Pichia pastoris
    • Fahnestock SR, Bedzyk LA, (1997) Production of synthetic spider dragline silk protein in Pichia pastoris. Appl Microbiol Biotechnol 47: 33-39.
    • (1997) Appl Microbiol Biotechnol , vol.47 , pp. 33-39
    • Fahnestock, S.R.1    Bedzyk, L.A.2
  • 8
    • 33745019144 scopus 로고    scopus 로고
    • Expression of spider flagelliform silk protein in Bombyx mori cell line by a novel Bac-to-Bac/BmNPV baculovirus expression system
    • Miao Y, Zhang Y, Nakagaki K, Zhao T, Zhao A, et al. (2006) Expression of spider flagelliform silk protein in Bombyx mori cell line by a novel Bac-to-Bac/BmNPV baculovirus expression system. Appl Microbiol Biotechnol 71: 192-199.
    • (2006) Appl Microbiol Biotechnol , vol.71 , pp. 192-199
    • Miao, Y.1    Zhang, Y.2    Nakagaki, K.3    Zhao, T.4    Zhao, A.5
  • 9
    • 48249103129 scopus 로고    scopus 로고
    • Expression of EGFP-spider dragline silk fusion protein in BmN cells and larvae of silkworm showed the solubility is primary limit for dragline proteins yield
    • Zhang Y, Hu J, Miao Y, Zhao A, Zhao T, et al. (2008) Expression of EGFP-spider dragline silk fusion protein in BmN cells and larvae of silkworm showed the solubility is primary limit for dragline proteins yield. Mol Biol Rep 35: 329-335.
    • (2008) Mol Biol Rep , vol.35 , pp. 329-335
    • Zhang, Y.1    Hu, J.2    Miao, Y.3    Zhao, A.4    Zhao, T.5
  • 10
    • 67049119193 scopus 로고    scopus 로고
    • Solution structure of eggcase silk protein and its implications for silk fiber formation
    • Lin Z, Huang W, Zhang J, Fan JS, Yang D, (2009) Solution structure of eggcase silk protein and its implications for silk fiber formation. Proc Natl Acad Sci U S A 106: 8906-8911.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 8906-8911
    • Lin, Z.1    Huang, W.2    Zhang, J.3    Fan, J.S.4    Yang, D.5
  • 11
    • 77951953534 scopus 로고    scopus 로고
    • A proposed model for dragline spider silk self-assembly: insights from the effect of the repetitive domain size on fiber properties
    • Ittah S, Barak N, Gat U, (2010) A proposed model for dragline spider silk self-assembly: insights from the effect of the repetitive domain size on fiber properties. Biopolymers 93: 458-468.
    • (2010) Biopolymers , vol.93 , pp. 458-468
    • Ittah, S.1    Barak, N.2    Gat, U.3
  • 12
    • 64149121998 scopus 로고    scopus 로고
    • Self-assembly of genetically engineered spider silk block copolymers
    • Rabotyagova OS, Cebe P, Kaplan DL, (2009) Self-assembly of genetically engineered spider silk block copolymers. Biomacromolecules 10: 229-236.
    • (2009) Biomacromolecules , vol.10 , pp. 229-236
    • Rabotyagova, O.S.1    Cebe, P.2    Kaplan, D.L.3
  • 13
    • 9244235033 scopus 로고    scopus 로고
    • Novel assembly properties of recombinant spider dragline silk proteins
    • Huemmerich D, Scheibel T, Vollrath F, Cohen S, Gat U, et al. (2004) Novel assembly properties of recombinant spider dragline silk proteins. Curr Biol 14: 2070-2074.
    • (2004) Curr Biol , vol.14 , pp. 2070-2074
    • Huemmerich, D.1    Scheibel, T.2    Vollrath, F.3    Cohen, S.4    Gat, U.5
  • 15
    • 0037127063 scopus 로고    scopus 로고
    • Spider silk fibers spun from soluble recombinant silk produced in mammalian cells
    • Lazaris A, Arcidiacono S, Huang Y, Zhou JF, Duguay F, et al. (2002) Spider silk fibers spun from soluble recombinant silk produced in mammalian cells. Science 295: 472-476.
    • (2002) Science , vol.295 , pp. 472-476
    • Lazaris, A.1    Arcidiacono, S.2    Huang, Y.3    Zhou, J.F.4    Duguay, F.5
  • 16
    • 34249889559 scopus 로고    scopus 로고
    • Macroscopic fibers self-assembled from recombinant miniature spider silk proteins
    • Stark M, Grip S, Rising A, Hedhammar M, Engstrom W, et al. (2007) Macroscopic fibers self-assembled from recombinant miniature spider silk proteins. Biomacromolecules 8: 1695-1701.
    • (2007) Biomacromolecules , vol.8 , pp. 1695-1701
    • Stark, M.1    Grip, S.2    Rising, A.3    Hedhammar, M.4    Engstrom, W.5
  • 17
    • 33745633089 scopus 로고    scopus 로고
    • An essential role for the C-terminal domain of a dragline spider silk protein in directing fiber formation
    • Ittah S, Cohen S, Garty S, Cohn D, Gat U, (2006) An essential role for the C-terminal domain of a dragline spider silk protein in directing fiber formation. Biomacromolecules 7: 1790-1795.
    • (2006) Biomacromolecules , vol.7 , pp. 1790-1795
    • Ittah, S.1    Cohen, S.2    Garty, S.3    Cohn, D.4    Gat, U.5
  • 18
    • 77952378056 scopus 로고    scopus 로고
    • A conserved spider silk domain acts as a molecular switch that controls fibre assembly
    • Hagn F, Eisoldt L, Hardy JG, Vendrely C, Coles M, et al. (2010) A conserved spider silk domain acts as a molecular switch that controls fibre assembly. Nature 465: 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
  • 19
    • 70349783566 scopus 로고    scopus 로고
    • Spider silk: from soluble protein to extraordinary fiber
    • Heim M, Keerl D, Scheibel T, (2009) Spider silk: from soluble protein to extraordinary fiber. Angew Chem Int Ed Engl 48: 3584-3596.
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 3584-3596
    • Heim, M.1    Keerl, D.2    Scheibel, T.3
  • 22
    • 13644260108 scopus 로고    scopus 로고
    • Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins
    • Scheibel T, (2004) Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins. Microb Cell Fact 3: 14.
    • (2004) Microb Cell Fact , vol.3 , pp. 14
    • Scheibel, T.1
  • 23
    • 78650419146 scopus 로고    scopus 로고
    • Diversity of molecular transformations involved in the formation of spider silks
    • Lefevre T, Boudreault S, Cloutier C, Pezolet M, (2011) Diversity of molecular transformations involved in the formation of spider silks. J Mol Biol 405: 238-253.
    • (2011) J Mol Biol , vol.405 , pp. 238-253
    • Lefevre, T.1    Boudreault, S.2    Cloutier, C.3    Pezolet, M.4
  • 24
    • 77951977674 scopus 로고    scopus 로고
    • Characterization of recombinantly produced spider flagelliform silk domains
    • Heim M, Ackerschott CB, Scheibel T, (2010) Characterization of recombinantly produced spider flagelliform silk domains. J Struct Biol 170: 420-425.
    • (2010) J Struct Biol , vol.170 , pp. 420-425
    • Heim, M.1    Ackerschott, C.B.2    Scheibel, T.3
  • 25
    • 4944247871 scopus 로고    scopus 로고
    • Molecular and mechanical characterization of aciniform silk: uniformity of iterated sequence modules in a novel member of the spider silk fibroin gene family
    • Hayashi CY, Blackledge TA, Lewis RV, (2004) Molecular and mechanical characterization of aciniform silk: uniformity of iterated sequence modules in a novel member of the spider silk fibroin gene family. Mol Biol Evol 21: 1950-1959.
    • (2004) Mol Biol Evol , vol.21 , pp. 1950-1959
    • Hayashi, C.Y.1    Blackledge, T.A.2    Lewis, R.V.3
  • 26
    • 6344228390 scopus 로고    scopus 로고
    • Primary structure elements of spider dragline silks and their contribution to protein solubility
    • Huemmerich D, Helsen CW, Quedzuweit S, Oschmann J, Rudolph R, et al. (2004) Primary structure elements of spider dragline silks and their contribution to protein solubility. Biochemistry 43: 13604-13612.
    • (2004) Biochemistry , vol.43 , pp. 13604-13612
    • Huemmerich, D.1    Helsen, C.W.2    Quedzuweit, S.3    Oschmann, J.4    Rudolph, R.5
  • 27
    • 0030042763 scopus 로고    scopus 로고
    • Methods to estimate the conformation of proteins and polypeptides from circular dichroism data
    • Greenfield NJ, (1996) Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Anal Biochem 235: 1-10.
    • (1996) Anal Biochem , vol.235 , pp. 1-10
    • Greenfield, N.J.1
  • 28
    • 40849102539 scopus 로고    scopus 로고
    • Structural properties of recombinant nonrepetitive and repetitive parts of major ampullate spidroin 1 from Euprosthenops australis: implications for fiber formation
    • Hedhammar M, Rising A, Grip S, Martinez AS, Nordling K, et al. (2008) Structural properties of recombinant nonrepetitive and repetitive parts of major ampullate spidroin 1 from Euprosthenops australis: implications for fiber formation. Biochemistry 47: 3407-3417.
    • (2008) Biochemistry , vol.47 , pp. 3407-3417
    • Hedhammar, M.1    Rising, A.2    Grip, S.3    Martinez, A.S.4    Nordling, K.5
  • 29
    • 68849091105 scopus 로고    scopus 로고
    • Engineered disulfides improve mechanical properties of recombinant spider silk
    • Grip S, Johansson J, Hedhammar M, (2009) Engineered disulfides improve mechanical properties of recombinant spider silk. Protein Sci 18: 1012-1022.
    • (2009) Protein Sci , vol.18 , pp. 1012-1022
    • Grip, S.1    Johansson, J.2    Hedhammar, M.3
  • 30
    • 50949132083 scopus 로고    scopus 로고
    • Processing conditions for the formation of spider silk microspheres
    • Lammel A, Schwab M, Slotta U, Winter G, Scheibel T, (2008) Processing conditions for the formation of spider silk microspheres. ChemSusChem 1: 413-416.
    • (2008) ChemSusChem , vol.1 , pp. 413-416
    • Lammel, A.1    Schwab, M.2    Slotta, U.3    Winter, G.4    Scheibel, T.5
  • 31
    • 0042364941 scopus 로고    scopus 로고
    • Mechanism of silk processing in insects and spiders
    • Jin HJ, Kaplan DL, (2003) Mechanism of silk processing in insects and spiders. Nature 424: 1057-1061.
    • (2003) Nature , vol.424 , pp. 1057-1061
    • Jin, H.J.1    Kaplan, D.L.2
  • 32
    • 77955310355 scopus 로고    scopus 로고
    • Molecular and nanostructural mechanisms of deformation, strength and toughness of spider silk fibrils
    • Nova A, Keten S, Pugno NM, Redaelli A, Buehler MJ, (2010) Molecular and nanostructural mechanisms of deformation, strength and toughness of spider silk fibrils. Nano Lett 10: 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
  • 33
    • 80755159083 scopus 로고    scopus 로고
    • Nanoconfinement of spider silk fibrils begets superior strength, extensibility, and toughness
    • Giesa T, Arslan M, Pugno NM, Buehler MJ, (2011) Nanoconfinement of spider silk fibrils begets superior strength, extensibility, and toughness. Nano Lett 11: 5038-5046.
    • (2011) Nano Lett , vol.11 , pp. 5038-5046
    • Giesa, T.1    Arslan, M.2    Pugno, N.M.3    Buehler, M.J.4
  • 34
    • 70350059595 scopus 로고    scopus 로고
    • Conformation and orientation of proteins in various types of silk fibers produced by Nephila clavipes spiders
    • Rousseau ME, Lefevre T, Pezolet M, (2009) Conformation and orientation of proteins in various types of silk fibers produced by Nephila clavipes spiders. Biomacromolecules 10: 2945-2953.
    • (2009) Biomacromolecules , vol.10 , pp. 2945-2953
    • Rousseau, M.E.1    Lefevre, T.2    Pezolet, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.