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Volumn 29, Issue 44, 2013, Pages 13457-13464

Tuning the self-assembly of short peptides via sequence variations

Author keywords

[No Author keywords available]

Indexed keywords

CRYOGENIC TRANSMISSION ELECTRON MICROSCOPY (CRYO-TEM); ELECTROSTATIC REPULSION; MOLECULAR DYNAMICS SIMULATIONS; NON-COVALENT INTERACTION; ONE-DIMENSIONAL NANOSTRUCTURE; PEPTIDE SELF ASSEMBLIES; SELF ASSEMBLED STRUCTURES; SMALL-ANGLE NEUTRON SCATTERING;

EID: 84887577182     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la402441w     Document Type: Article
Times cited : (147)

References (53)
  • 1
    • 0037192455 scopus 로고    scopus 로고
    • Toward self-organization and complex matter
    • Lehn, J. M. Toward self-organization and complex matter Science 2002, 295, 2400-2403
    • (2002) Science , vol.295 , pp. 2400-2403
    • Lehn, J.M.1
  • 2
    • 0037192505 scopus 로고    scopus 로고
    • Self-assembly at all scales
    • Whitesides, G. M.; Grzybowski, B. Self-assembly at all scales Science 2002, 295, 2418-2421
    • (2002) Science , vol.295 , pp. 2418-2421
    • Whitesides, G.M.1    Grzybowski, B.2
  • 3
    • 0037117591 scopus 로고    scopus 로고
    • Beyond molecules: Self-assembly of mesoscopic and macroscopic components
    • Whitesides, G. M.; Boncheva, M. Beyond molecules: Self-assembly of mesoscopic and macroscopic components Proc. Natl. Acad. Sci. U. S. A. 2002, 99, 4769-4774
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 4769-4774
    • Whitesides, G.M.1    Boncheva, M.2
  • 4
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of novel biomaterials through molecular self-assembly
    • Zhang, S. Fabrication of novel biomaterials through molecular self-assembly Nat. Biotechnol. 2003, 21, 1711-1178
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1711-1178
    • Zhang, S.1
  • 5
    • 34547316314 scopus 로고    scopus 로고
    • Self-assembled peptide nanostructures: The design of molecular building blocks and their technological utilization
    • Gazit, E. Self-assembled peptide nanostructures: The design of molecular building blocks and their technological utilization Chem. Soc. Rev. 2007, 36, 1263-1269
    • (2007) Chem. Soc. Rev. , vol.36 , pp. 1263-1269
    • Gazit, E.1
  • 6
    • 41149104937 scopus 로고    scopus 로고
    • Designing peptide based nanomaterials
    • Ulijn, R. V.; Smith, A. M. Designing peptide based nanomaterials Chem. Soc. Rev. 2008, 37, 664-675
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 664-675
    • Ulijn, R.V.1    Smith, A.M.2
  • 7
    • 77952850295 scopus 로고    scopus 로고
    • Self-assembly and application of diphenylalanine-based nanostructures
    • Yan, X.; Zhu, P.; Li, J. Self-assembly and application of diphenylalanine-based nanostructures Chem. Soc. Rev. 2010, 39, 1877-1890
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 1877-1890
    • Yan, X.1    Zhu, P.2    Li, J.3
  • 9
    • 77950342360 scopus 로고    scopus 로고
    • Self-assembly of peptide amphiphiles: From molecules to nanostructures to biomaterials
    • Cui, H.; Webber, M. J.; Stupp, S. I. Self-assembly of peptide amphiphiles: From molecules to nanostructures to biomaterials Biopolymers 2010, 94, 1-18
    • (2010) Biopolymers , vol.94 , pp. 1-18
    • Cui, H.1    Webber, M.J.2    Stupp, S.I.3
  • 10
    • 79954995146 scopus 로고    scopus 로고
    • Self-assembly of amphiphilic peptides
    • Hamley, I. W. Self-assembly of amphiphilic peptides Soft Matter 2011, 7, 4122-4138
    • (2011) Soft Matter , vol.7 , pp. 4122-4138
    • Hamley, I.W.1
  • 12
    • 79958780734 scopus 로고    scopus 로고
    • Ultrasmall natural peptides self-assemble to strong temperature-resistant helical fibers in scaffolds suitable for tissue engineering
    • Mishra, A.; Loo, Y.; Deng, R.; Chuah, Y. J.; Hee, H. T.; Ying, J. Y.; Hauser, C. A. E. Ultrasmall natural peptides self-assemble to strong temperature-resistant helical fibers in scaffolds suitable for tissue engineering Nano Today 2011, 6, 232-239
    • (2011) Nano Today , vol.6 , pp. 232-239
    • Mishra, A.1    Loo, Y.2    Deng, R.3    Chuah, Y.J.4    Hee, H.T.5    Ying, J.Y.6    Hauser, C.A.E.7
  • 13
    • 84055193706 scopus 로고    scopus 로고
    • 6D adopt α-helical structures useful for membrane protein stabilization
    • 6D adopt α-helical structures useful for membrane protein stabilization Membranes 2011, 1, 314-326
    • (2011) Membranes , vol.1 , pp. 314-326
    • Zhuang, F.1    Ogleì̈cka, K.2    Hauser, C.A.E.3
  • 14
    • 84872201218 scopus 로고    scopus 로고
    • Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis
    • Lakshmanana, A.; Cheong, D. W.; Accardo, A.; Di Fabrizio, E.; Riekel, C.; Hauser, C. A. E. Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis Proc. Natl. Acad. Sci. U. S. A. 2013, 110, 519-524
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 519-524
    • Lakshmanana, A.1    Cheong, D.W.2    Accardo, A.3    Di Fabrizio, E.4    Riekel, C.5    Hauser, C.A.E.6
  • 15
    • 0027416047 scopus 로고
    • Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane
    • Zhang, S.; Holmes, T.; Lockshin, C.; Rich, A. Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane Proc. Natl. Acad. Sci. U. S. A. 1993, 90, 3334-3338
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 3334-3338
    • Zhang, S.1    Holmes, T.2    Lockshin, C.3    Rich, A.4
  • 16
    • 0037466613 scopus 로고    scopus 로고
    • Casting metal nanowires within discrete self-assembled peptide nanotubes
    • Reches, M.; Gazit, E. Casting metal nanowires within discrete self-assembled peptide nanotubes Science 2003, 300, 625-627
    • (2003) Science , vol.300 , pp. 625-627
    • Reches, M.1    Gazit, E.2
  • 18
    • 34250841766 scopus 로고    scopus 로고
    • Transition of cationic dipeptide nanotubes into vesicles and oligonucleotide delivery
    • Yan, X.; He, Q.; Wang, K.; Duan, L.; Cui, Y.; Li, J. Transition of cationic dipeptide nanotubes into vesicles and oligonucleotide delivery Angew. Chem., Int. Ed. 2007, 46, 2431-2434
    • (2007) Angew. Chem., Int. Ed. , vol.46 , pp. 2431-2434
    • Yan, X.1    He, Q.2    Wang, K.3    Duan, L.4    Cui, Y.5    Li, J.6
  • 20
    • 80555144149 scopus 로고    scopus 로고
    • Self-assembly of short peptide amphiphiles: The cooperative effect of hydrophobic interaction and hydrogen bonding
    • Han, S.; Cao, S.; Wang, Y.; Wang, J.; Xia, D.; Xu, H.; Zhao, X.; Lu, J. R. Self-assembly of short peptide amphiphiles: The cooperative effect of hydrophobic interaction and hydrogen bonding Chem.-Eur. J. 2011, 17, 13095-13102
    • (2011) Chem. - Eur. J. , vol.17 , pp. 13095-13102
    • Han, S.1    Cao, S.2    Wang, Y.3    Wang, J.4    Xia, D.5    Xu, H.6    Zhao, X.7    Lu, J.R.8
  • 21
    • 76249110195 scopus 로고    scopus 로고
    • Antibacterial activities of short designer peptides: A link between propensity for nanostructuring and capacity for membrane destabilization
    • Chen, C.; Pan, F.; Zhang, S.; Hu, J.; Cao, M.; Wang, J.; Xu, H.; Zhao, X.; Lu, J. R. Antibacterial activities of short designer peptides: A link between propensity for nanostructuring and capacity for membrane destabilization Biomacromolecules 2010, 11, 402-411
    • (2010) Biomacromolecules , vol.11 , pp. 402-411
    • Chen, C.1    Pan, F.2    Zhang, S.3    Hu, J.4    Cao, M.5    Wang, J.6    Xu, H.7    Zhao, X.8    Lu, J.R.9
  • 22
    • 80055106640 scopus 로고    scopus 로고
    • Molecular mechanisms of antibacterial and antitumor actions of designed surfactant-like peptides
    • Chen, C.; Hu, J.; Zhang, S.; Zhou, P.; Zhao, X.; Xu, H.; Zhao, X.; Yaseen, M.; Lu, J. R. Molecular mechanisms of antibacterial and antitumor actions of designed surfactant-like peptides Biomaterials 2012, 33, 592-603
    • (2012) Biomaterials , vol.33 , pp. 592-603
    • Chen, C.1    Hu, J.2    Zhang, S.3    Zhou, P.4    Zhao, X.5    Xu, H.6    Zhao, X.7    Yaseen, M.8    Lu, J.R.9
  • 25
    • 79955644016 scopus 로고    scopus 로고
    • Mechanistic processes underlying biomimetic synthesis of silica nanotubes from self-assembled ultrashort peptide templates
    • Wang, S.; Ge, X.; Xue, J.; Fan, H.; Mu, L.; Li, Y.; Xu, H.; Lu, J. R. Mechanistic processes underlying biomimetic synthesis of silica nanotubes from self-assembled ultrashort peptide templates Chem. Mater. 2011, 23, 2466-2474
    • (2011) Chem. Mater. , vol.23 , pp. 2466-2474
    • Wang, S.1    Ge, X.2    Xue, J.3    Fan, H.4    Mu, L.5    Li, Y.6    Xu, H.7    Lu, J.R.8
  • 26
    • 84865255381 scopus 로고    scopus 로고
    • Biomimetic synthesis of silica nanostructures with controllable morphologies and sizes through tuning interfacial interactions
    • Wang, S.; Xue, J.; Ge, X.; Fan, H.; Xu, H.; Lu, J. R. Biomimetic synthesis of silica nanostructures with controllable morphologies and sizes through tuning interfacial interactions Chem. Commun. 2012, 48, 9415-9417
    • (2012) Chem. Commun. , vol.48 , pp. 9415-9417
    • Wang, S.1    Xue, J.2    Ge, X.3    Fan, H.4    Xu, H.5    Lu, J.R.6
  • 29
    • 0030569147 scopus 로고    scopus 로고
    • Scattering functions of semiflexible polymers with and without excluded volume effects
    • Pedersen, J. S.; Schurtenberger, P. Scattering functions of semiflexible polymers with and without excluded volume effects Macromolecules 1996, 29, 7602-7612
    • (1996) Macromolecules , vol.29 , pp. 7602-7612
    • Pedersen, J.S.1    Schurtenberger, P.2
  • 30
    • 33746598949 scopus 로고    scopus 로고
    • Incorporating intermicellar interactions in the fitting of SANS data form cationic wormlike micelles
    • Chen, W.-R.; Butler, P. D.; Magid, L. J. Incorporating intermicellar interactions in the fitting of SANS data form cationic wormlike micelles Langmuir 2006, 22, 6539-6548
    • (2006) Langmuir , vol.22 , pp. 6539-6548
    • Chen, W.-R.1    Butler, P.D.2    Magid, L.J.3
  • 33
    • 33645941402 scopus 로고
    • The OPLS potential functions for proteins. Energy minimizations for crystals of cyclic peptides and crambin
    • Jorgensen, W. L.; Tirado-Rives, J. The OPLS potential functions for proteins. Energy minimizations for crystals of cyclic peptides and crambin J. Am. Chem. Soc. 1988, 110, 1657-1666
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 35
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N ·log(N) method for Ewald sums in large systems
    • Darden, T.; York, D.; Pedersen, L. Particle mesh Ewald: An N ·log(N) method for Ewald sums in large systems J. Chem. Phys. 1993, 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 37
    • 84943502952 scopus 로고
    • A molecular dynamics method for simulations in the canonical ensemble
    • Nose, S. A molecular dynamics method for simulations in the canonical ensemble Mol. Phys. 1984, 52, 255-268
    • (1984) Mol. Phys. , vol.52 , pp. 255-268
    • Nose, S.1
  • 38
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover, W. G. Canonical dynamics: Equilibrium phase-space distributions Phys. Rev. A: At., Mol., Opt. Phys. 1985, 31, 1695-1697
    • (1985) Phys. Rev. A: At., Mol., Opt. Phys. , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 39
    • 0028176595 scopus 로고
    • Measurement of the β-sheet-forming propensities of amino acids
    • Minor, L. J. D.; Kim, S. P. Measurement of the β-sheet-forming propensities of amino acids Nature 1994, 367, 660-663
    • (1994) Nature , vol.367 , pp. 660-663
    • Minor, L.J.D.1    Kim, S.P.2
  • 40
    • 0029064713 scopus 로고
    • Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides
    • Xiong, H.; Buckwalter, B. L.; Shieh, H. M.; Hecht, M. H. Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides Proc. Natl. Acad. Sci. U. S. A. 1995, 92, 6349-6353
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 6349-6353
    • Xiong, H.1    Buckwalter, B.L.2    Shieh, H.M.3    Hecht, M.H.4
  • 41
  • 43
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • Levine, H. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution Protein Sci. 1993, 2, 404-410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • Levine, H.1
  • 44
    • 0037592927 scopus 로고    scopus 로고
    • Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence
    • Ban, T.; Hamada, D.; Hasegawa, K.; Naiki, H.; Goto, Y. Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence J. Biol. Chem. 2003, 278, 16462-16465
    • (2003) J. Biol. Chem. , vol.278 , pp. 16462-16465
    • Ban, T.1    Hamada, D.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5
  • 45
    • 58149326746 scopus 로고    scopus 로고
    • Molecular mechanism of thioflavin-T binding to the surface of β-rich peptide self-assemblies
    • Biancalana, M.; Makabe, K.; Koide, A.; Koide, S. Molecular mechanism of thioflavin-T binding to the surface of β-rich peptide self-assemblies J. Mol. Biol. 2009, 385, 1052-1063
    • (2009) J. Mol. Biol. , vol.385 , pp. 1052-1063
    • Biancalana, M.1    Makabe, K.2    Koide, A.3    Koide, S.4
  • 46
    • 70349900704 scopus 로고    scopus 로고
    • Controllable peptide-dendron self-assembly: Interconversion of nanotubes and fibrillar nanostructures
    • Shao, H.; Parquette, J. R. Controllable peptide-dendron self-assembly: Interconversion of nanotubes and fibrillar nanostructures Angew. Chem., Int. Ed. 2009, 48, 2525-2528
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 2525-2528
    • Shao, H.1    Parquette, J.R.2
  • 49
    • 79952265946 scopus 로고    scopus 로고
    • Unraveling the mechanism of nanotube formation by chiral self-assembly of amphiphiles
    • Ziserman, L.; Lee, H.-Y.; Raghavan, S. R.; Mor, A.; Danino, D. Unraveling the mechanism of nanotube formation by chiral self-assembly of amphiphiles J. Am. Chem. Soc. 2011, 133, 2511-2517
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2511-2517
    • Ziserman, L.1    Lee, H.-Y.2    Raghavan, S.R.3    Mor, A.4    Danino, D.5
  • 50
    • 0000111757 scopus 로고    scopus 로고
    • Fibril stability in solutions of twisted β-sheet peptides: A new kind of micellization in chiral systems
    • Nyrkova, I. A.; Semenov, A. N.; Aggeli, A.; Boden, N. Fibril stability in solutions of twisted β-sheet peptides: A new kind of micellization in chiral systems Eur. Phys. J. B 2000, 17, 481-497
    • (2000) Eur. Phys. J. B , vol.17 , pp. 481-497
    • Nyrkova, I.A.1    Semenov, A.N.2    Aggeli, A.3    Boden, N.4
  • 53
    • 33947423449 scopus 로고    scopus 로고
    • The internal structure of self-assembled peptide amphiphiles nanofibers
    • Jiang, H. Z.; Guler, M. O.; Stupp, S. I. The internal structure of self-assembled peptide amphiphiles nanofibers Soft Matter 2007, 3, 454-462
    • (2007) Soft Matter , vol.3 , pp. 454
    • Jiang, H.Z.1    Guler, M.O.2    Stupp, S.I.3


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