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Volumn 109, Issue 29, 2012, Pages 11657-11662

Self-assembly of tunable protein suprastructures from recombinant oleosin

Author keywords

Cryogenic transmission microscopy; Protein surfactants; Self assembled suprastructure

Indexed keywords

CALCEIN; MUTANT PROTEIN; NANOMATERIAL; RECOMBINANT OLEOSIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 84863918531     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1205426109     Document Type: Article
Times cited : (95)

References (41)
  • 1
    • 0022832167 scopus 로고
    • Giant vesicle bilayers composed of mixtures of lipids, cholesterol and polypeptides - Thermomechanical and (mutual) adherence properties
    • Evans E, Needham D (1986) Giant vesicle bilayers composed of mixtures of lipids, cholesterol and polypeptides - Thermomechanical and (mutual) adherence properties. Faraday Discuss Chem Soc 81:267-280.
    • (1986) Faraday Discuss Chem Soc , vol.81 , pp. 267-280
    • Evans, E.1    Needham, D.2
  • 2
    • 1642362625 scopus 로고    scopus 로고
    • Drug Delivery Systems: Entering the Mainstream
    • DOI 10.1126/science.1095833
    • Allen TM, Cullis PR (2004) Drug delivery systems: Entering the mainstream. Science 303:1818-1822. (Pubitemid 38374867)
    • (2004) Science , vol.303 , Issue.5665 , pp. 1818-1822
    • Allen, T.M.1    Cullis, P.R.2
  • 3
    • 4444340443 scopus 로고
    • Block copolymer thermodynamics - Theory and experiment
    • Bates FS, Fredrickson GH (1990) Block copolymer thermodynamics - Theory and experiment. Annu Rev Phys Chem 41:525-557.
    • (1990) Annu Rev Phys Chem , vol.41 , pp. 525-557
    • Bates, F.S.1    Fredrickson, G.H.2
  • 5
    • 77953076879 scopus 로고    scopus 로고
    • Self-assembly of janus dendrimers into uniform dendrimersomes and other complex architectures
    • Percec V, et al. (2010) Self-assembly of janus dendrimers into uniform dendrimersomes and other complex architectures. Science 328:1009-1014.
    • (2010) Science , vol.328 , pp. 1009-1014
    • Percec, V.1
  • 7
    • 13944260441 scopus 로고    scopus 로고
    • Reversible inside-out micellization of pH-responsive and water-soluble vesicles based on polypeptide diblock copolymers
    • DOI 10.1021/ja043920g
    • Rodriguez-Hernandez J, Lecommandoux S (2005) Reversible inside-out micellization of pH-responsive and water-soluble vesicles based on polypeptide diblock copolymers. J Am Chem Soc 127:2026-2027. (Pubitemid 40270489)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.7 , pp. 2026-2027
    • Rodriguez-Hernandez, J.1    Lecommandoux, S.2
  • 8
    • 77952754156 scopus 로고    scopus 로고
    • Synthesis and cross linking of L-DOPA containing polypeptide vesicles
    • Holowka EP, Deming TJ (2010) Synthesis and cross linking of L-DOPA containing polypeptide vesicles. Macromol Biosci 10:496-502.
    • (2010) Macromol Biosci , vol.10 , pp. 496-502
    • Holowka, E.P.1    Deming, T.J.2
  • 10
    • 77950354591 scopus 로고    scopus 로고
    • Elastin-like polypeptides: Biomedical applications of tunable biopolymers
    • MacEwan SR, Chilkoti A (2010) Elastin-like polypeptides: Biomedical applications of tunable biopolymers. Biopolymers 94:60-77.
    • (2010) Biopolymers , vol.94 , pp. 60-77
    • MacEwan, S.R.1    Chilkoti, A.2
  • 12
    • 84856848176 scopus 로고    scopus 로고
    • Temperature-triggered self-assembly of elastin-like block co-recombinamers: The controlled formation of micelles and vesicles in an aqueous medium
    • Martin L, Castro E, Ribeiro A, AlonsoM, Rodriguez-Cabello JC (2012) Temperature-triggered self-assembly of elastin-like block co-recombinamers: The controlled formation of micelles and vesicles in an aqueous medium. Biomacromolecules 13:293-298.
    • (2012) Biomacromolecules , vol.13 , pp. 293-298
    • Martin, L.1    Castro, E.2    Ribeiro, A.3    Alonso, M.4    Rodriguez-Cabello, J.C.5
  • 13
    • 0027140232 scopus 로고
    • Interfacial self-assembly of a fungal hydrophobin into a hydrophobic rodlet layer
    • DOI 10.1105/tpc.5.11.1567
    • Wosten HAB, Devries OMH, Wessels JGH (1993) Interfacial self-assembly of a fungal hydrophobin into a hydrophobic rodlet layer. Plant Cell 5:1567-1574. (Pubitemid 2021803)
    • (1993) Plant Cell , vol.5 , Issue.11 , pp. 1567-1574
    • Wosten, H.A.B.1    De Vries, O.M.H.2    Wessels, J.G.H.3
  • 14
    • 0000265898 scopus 로고
    • Oil bodies and oleosins in seeds
    • Huang AHC (1992) Oil bodies and oleosins in seeds. Annu Rev Plant Phys 43:177-200.
    • (1992) Annu Rev Plant Phys , vol.43 , pp. 177-200
    • Huang, A.H.C.1
  • 15
    • 0022491826 scopus 로고
    • Isolation and characterization of latherin, a surface-active protein from horse sweat
    • Beeley JG, Eason R, Snow DH (1986) Isolation and characterization of latherin, a surface- active protein from horse sweat. Biochem J 235:645-650. (Pubitemid 16071971)
    • (1986) Biochemical Journal , vol.235 , Issue.3 , pp. 645-650
    • Beeley, J.G.1    Eason, R.2    Snow, D.H.3
  • 16
    • 52649163989 scopus 로고    scopus 로고
    • Novel surfactant proteins are involved in the structure and stability of foam nests from the frog Leptodactylus vastus
    • Hissa DC, et al. (2008) Novel surfactant proteins are involved in the structure and stability of foam nests from the frog Leptodactylus vastus. J Exp Biol 211:2707-2711.
    • (2008) J Exp Biol , vol.211 , pp. 2707-2711
    • Hissa, D.C.1
  • 17
    • 0036938740 scopus 로고    scopus 로고
    • Targeting and membrane-insertion of a sunflower oleosin in vitro and in Saccharomyces cerevisiae: The central hydrophobic domain contains more than one signal sequence, and directs oleosin insertion into the endoplasmic reticulum membrane using a signal anchor sequence mechanism
    • DOI 10.1007/s00425-002-0737-1
    • Beaudoin F, Napier JA (2002) Targeting and membrane-insertion of a sunflower oleosin in vitro and in Saccharomyces cerevisiae: The central hydrophobic domain contains more than one signal sequence, and directs oleosin insertion into the endoplasmic reticulum membrane using a signal anchor sequence mechanism. Planta 215:293-303. (Pubitemid 36064979)
    • (2002) Planta , vol.215 , Issue.2 , pp. 293-303
    • Beaudoin, F.1    Napier, J.A.2
  • 18
    • 0032168202 scopus 로고    scopus 로고
    • Secondary structure of oleosins in oil bodies isolated from seeds of safflower (Carthamus tinctorius L.) and sunflower (Helianthus annuus L.)
    • Lacey DJ, Wellner N, Beaudoin F, Napier JA, Shewry PR (1998) Secondary structure of oleosins in oil bodies isolated from seeds of safflower (Carthamus tinctorius L) and sunflower (Helianthus annuus L). Biochem J 334:469-477. (Pubitemid 28448592)
    • (1998) Biochemical Journal , vol.334 , Issue.2 , pp. 469-477
    • Lacey, D.J.1    Wellner, N.2    Beaudoin, F.3    Napier, J.A.4    Shewry, P.R.5
  • 19
    • 16544370489 scopus 로고    scopus 로고
    • Endoplasmic reticulum, oleosins, and oils in seeds and tapetum cells
    • DOI 10.1104/pp.104.051060
    • Hsieh K, Huang AHC (2004) Endoplasmic reticulum, oleosins, and oils in seeds and tapetum cells. Plant Physiol 136:3427-3434. (Pubitemid 41075782)
    • (2004) Plant Physiology , vol.136 , Issue.3 , pp. 3427-3434
    • Hsieh, K.1    Huang, A.H.C.2
  • 21
    • 0031201009 scopus 로고    scopus 로고
    • Role of the proline knot motif in oleosin endoplasmic reticulum topology and oil body targeting
    • DOI 10.1105/tpc.9.8.1481
    • Abell BM, et al. (1997) Role of the proline knot motif in oleosin endoplasmic reticulum topology and oil body targeting. Plant Cell 9:1481-1493. (Pubitemid 28174124)
    • (1997) Plant Cell , vol.9 , Issue.8 , pp. 1481-1493
    • Abell, B.M.1    Holbrook, L.A.2    Abenes, M.3    Murphy, D.J.4    Hills, M.J.5    Moloney, M.M.6
  • 22
    • 77949571450 scopus 로고    scopus 로고
    • Use of oil bodies and oleosins in recombinant protein production and other biotechnological applications
    • Bhatla SC, Kaushik V, Yadav MK (2010) Use of oil bodies and oleosins in recombinant protein production and other biotechnological applications. Biotechnol Adv 28:293-300.
    • (2010) Biotechnol Adv , vol.28 , pp. 293-300
    • Bhatla, S.C.1    Kaushik, V.2    Yadav, M.K.3
  • 23
    • 80053268007 scopus 로고    scopus 로고
    • Functionalized nanoscale oil bodies for targeted delivery of a hydrophobic drug
    • Chiang CJ, Lin CC, Lu TL, Wang HF (2011) Functionalized nanoscale oil bodies for targeted delivery of a hydrophobic drug. Nanotechnology 22:415102.
    • (2011) Nanotechnology , vol.22 , pp. 415102
    • Chiang, C.J.1    Lin, C.C.2    Lu, T.L.3    Wang, H.F.4
  • 24
    • 79251543643 scopus 로고    scopus 로고
    • Selective internalization of self-assembled artificial oil bodies by HER2/neu-positive cells
    • Chiang CJ, Lin LJ, Lin CC, Chang CH, Chao YP (2011) Selective internalization of self-assembled artificial oil bodies by HER2/neu-positive cells. Nanotechnology 22:015102.
    • (2011) Nanotechnology , vol.22 , pp. 015102
    • Chiang, C.J.1    Lin, L.J.2    Lin, C.C.3    Chang, C.H.4    Chao, Y.P.5
  • 25
    • 2942521049 scopus 로고    scopus 로고
    • A system for purification of recombinant proteins in Escherichia coli via artificial oil bodies constituted with their oleosin-fused polypeptides
    • DOI 10.1016/j.jbiotec.2004.03.013, PII S0168165604001804
    • Peng CC, Chen JCF, Shyu DJH, Chen MJ, Tzen JIC (2004) A system for purification of recombinant proteins in Escherichia coli via artificial oil bodies constituted with their oleosin-fused polypeptides. J Biotechnol 111:51-57. (Pubitemid 38757820)
    • (2004) Journal of Biotechnology , vol.111 , Issue.1 , pp. 51-57
    • Peng, C.-C.1    Chen, J.C.F.2    Shyu, D.J.H.3    Chen, M.-J.4    Tzen, J.T.C.5
  • 26
    • 77956469183 scopus 로고    scopus 로고
    • Elevation of oil body integrity and emulsion stability by polyoleosins, multiple oleosin units joined in tandem head-to-tail fusions
    • Scott RW, et al. (2010) Elevation of oil body integrity and emulsion stability by polyoleosins, multiple oleosin units joined in tandem head-to-tail fusions. Plant Biotechnol J 8:912-927.
    • (2010) Plant Biotechnol J , vol.8 , pp. 912-927
    • Scott, R.W.1
  • 27
    • 37349037151 scopus 로고    scopus 로고
    • Selective one-step extraction of Arabidopsis thaliana seed oleosins using organic solvents
    • D'andrea S, et al. (2007) Selective one-step extraction of Arabidopsis thaliana seed oleosins using organic solvents. J Agric Food Chem 55:10008-10015.
    • (2007) J Agric Food Chem , vol.55 , pp. 10008-10015
    • D'Andrea, S.1
  • 28
    • 0034925721 scopus 로고    scopus 로고
    • Large scale purification of an almond oleosin using an organic solvent procedure
    • DOI 10.1016/S0981-9428(01)01275-X
    • Beisson F, Ferte N, Voultoury R, Arondel V (2001) Large scale purification of an almond oleosin using an organic solvent procedure. Plant Physiol Bioch 39:623-630. (Pubitemid 32679725)
    • (2001) Plant Physiology and Biochemistry , vol.39 , Issue.7-8 , pp. 623-630
    • Beisson, F.1    Ferte, N.2    Voultoury, R.3    Arondel, V.4
  • 29
    • 0035917939 scopus 로고    scopus 로고
    • Preparation, stability, and in vitro performance of vesicles made with diblock copolymers
    • Lee JCM, et al. (2001) Preparation, stability, and in vitro performance of vesicles made with diblock copolymers. Biotechnol Bioeng 73:135-145.
    • (2001) Biotechnol Bioeng , vol.73 , pp. 135-145
    • Lee, J.C.M.1
  • 30
    • 41949123352 scopus 로고    scopus 로고
    • Hierarchically structuredmicroparticles formed by interfacial instabilities of emulsion droplets containing amphiphilic block copolymers
    • Zhu J, Hayward RC (2008) Hierarchically structuredmicroparticles formed by interfacial instabilities of emulsion droplets containing amphiphilic block copolymers. Angew Chem Int Edit Engl 47:2113-2116.
    • (2008) Angew Chem Int Edit Engl , vol.47 , pp. 2113-2116
    • Zhu, J.1    Hayward, R.C.2
  • 31
    • 0037018567 scopus 로고    scopus 로고
    • Cryogenic transmission electron microscopy (cryo-TEM) of micelles and vesicles formed in water by poly(ethylene oxide)-based block copolymers
    • DOI 10.1021/jp013639d
    • Won YY, Brannan AK, Davis HT, Bates FS (2002) Cryogenic transmission electron microscopy (Cryo-TEM) of micelles and vesicles formed in water by poly(ethylene oxide)-based block copolymers. J Phys Chem B 106:3354-3364. (Pubitemid 35290231)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.13 , pp. 3354-3364
    • Won, Y.-Y.1    Brannan, A.K.2    Davis, H.T.3    Bates, F.S.4
  • 33
    • 77955868837 scopus 로고    scopus 로고
    • Cryogenic transmission electron microscopy for direct observation of polymer and small-molecule materials and structures in solution
    • Zhong S, Pochan DJ (2010) Cryogenic transmission electron microscopy for direct observation of polymer and small-molecule materials and structures in solution. Polym Rev 50:287-320.
    • (2010) Polym Rev , vol.50 , pp. 287-320
    • Zhong, S.1    Pochan, D.J.2
  • 34
    • 0029252080 scopus 로고
    • Cryo-TEM evidence: Sonication of dihexadecyl phosphate does not produce closed bilayers with smooth curvature
    • Hammarstroem L, Velikian I, Karlsson G, Edwards K (1995) Cryo-TEM evidence: Sonication of dihexadecyl phosphate does not produce closed bilayers with smooth curvature. Langmuir 11:408-410.
    • (1995) Langmuir , vol.11 , pp. 408-410
    • Hammarstroem, L.1    Velikian, I.2    Karlsson, G.3    Edwards, K.4
  • 35
    • 0037044346 scopus 로고    scopus 로고
    • Molecular weight dependence of polymersome membrane structure, elasticity, and stability
    • DOI 10.1021/ma020669l
    • Bermudez H, Brannan AK, Hammer DA, Bates FS, Discher DE (2002) Molecular weight dependence of polymersome membrane structure, elasticity, and stability. Macromolecules 35:8203-8208. (Pubitemid 35173635)
    • (2002) Macromolecules , vol.35 , Issue.21 , pp. 8203-8208
    • Bermudez, H.1    Brannan, A.K.2    Hammer, D.A.3    Bates, F.S.4    Discher, D.E.5
  • 36
    • 2542613793 scopus 로고    scopus 로고
    • Rheology of block copolypeptide solutions: Hydrogels with tunable properties
    • Breedveld V, Nowak AP, Sato J, Deming TJ, Pine DJ (2004) Rheology of block copolypeptide solutions: Hydrogels with tunable properties. Macromolecules 37:3943-3953.
    • (2004) Macromolecules , vol.37 , pp. 3943-3953
    • Breedveld, V.1    Nowak, A.P.2    Sato, J.3    Deming, T.J.4    Pine, D.J.5
  • 38
  • 39
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • DOI 10.1006/abio.2000.4880
    • Sreerama N,Woody RW (2000) Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 287:252-260. (Pubitemid 32006234)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 40
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • DOI 10.1093/nar/gkh371
    • Whitmore L, Wallace BA (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 32:W668-W673. (Pubitemid 38997420)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Whitmore, L.1    Wallace, B.A.2
  • 41
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis
    • DOI 10.1006/abio.2000.4879
    • Sreerama N, Venyaminov SY,Woody RW (2000) Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis. Anal Biochem 287:243-251. (Pubitemid 32006233)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Yu.2    Woody, R.W.3


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