메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Ostwalds rule of stages governs structural transitions and morphology of dipeptide supramolecular polymers

Author keywords

[No Author keywords available]

Indexed keywords

DIPEPTIDE DERIVATIVE; DIPEPTIDE SUPRAMOLECULAR POLYMER; MONOMER; NANOMATERIAL; NANOSPHERE; POLYMER; UNCLASSIFIED DRUG; DIPEPTIDE; PEPTIDE NANOTUBE;

EID: 84928143653     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6219     Document Type: Article
Times cited : (201)

References (63)
  • 1
    • 0036809602 scopus 로고    scopus 로고
    • Supramolecular polymer chemistry-scope and perspectives
    • Lehn, J. M. Supramolecular polymer chemistry-scope and perspectives. Polym. Int. 51, 825-839 (2002).
    • (2002) Polym. Int. , vol.51 , pp. 825-839
    • Lehn, J.M.1
  • 3
    • 84857319239 scopus 로고    scopus 로고
    • Functional supramolecular polymers
    • Aida, T., Meijer, E. & Stupp, S. I. Functional supramolecular polymers. Science 335, 813-817 (2012).
    • (2012) Science , vol.335 , pp. 813-817
    • Aida, T.1    Meijer, E.2    Stupp, S.I.3
  • 4
    • 0037047627 scopus 로고    scopus 로고
    • Polymer vesicles
    • Discher, D. & Eisenberg, A. Polymer vesicles. Science 297, 967-973 (2002).
    • (2002) Science , vol.297 , pp. 967-973
    • Discher, D.1    Eisenberg, A.2
  • 5
    • 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. 21, 1171-1178 (2003).
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1171-1178
    • Zhang, S.1
  • 7
    • 0025668818 scopus 로고
    • Perspectives in supramolecular chemistry-from molecular recognition towards molecular information processing and self-organization
    • Lehn, J. M. Perspectives in supramolecular chemistry-from molecular recognition towards molecular information processing and self-organization. Angew. Chem. Int. Ed. 29, 1304-1319 (1990).
    • (1990) Angew. Chem. Int. Ed. , vol.29 , pp. 1304-1319
    • Lehn, J.M.1
  • 8
    • 79955453665 scopus 로고    scopus 로고
    • Optically healable supramolecular polymers
    • Burnworth, M. et al. Optically healable supramolecular polymers. Nature 472, 334-338 (2011).
    • (2011) Nature , vol.472 , pp. 334-338
    • Burnworth, M.1
  • 9
    • 2442718759 scopus 로고    scopus 로고
    • Synthesis of peptide-nanotube platinum-nanoparticle composites
    • Song, Y. et al. Synthesis of peptide-nanotube platinum-nanoparticle composites. Chem. Commun. 7, 1044-1045 (2004).
    • (2004) Chem. Commun. , vol.7 , pp. 1044-1045
    • Song, Y.1
  • 10
    • 84866096280 scopus 로고    scopus 로고
    • Characterization of supramolecular polymers
    • Liu, Y., Wang, Z. & Zhang, X. Characterization of supramolecular polymers. Chem. Soc. Rev. 41, 5922-5932 (2012).
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 5922-5932
    • Liu, Y.1    Wang, Z.2    Zhang, X.3
  • 11
    • 84870416506 scopus 로고    scopus 로고
    • Coassembly of aromatic dipeptides into biomolecular necklaces
    • Yuran, S., Razvag, Y. & Reches, M. Coassembly of aromatic dipeptides into biomolecular necklaces. ACS Nano 6, 9559-9566 (2012).
    • (2012) ACS Nano , vol.6 , pp. 9559-9566
    • Yuran, S.1    Razvag, Y.2    Reches, M.3
  • 12
    • 84857645441 scopus 로고    scopus 로고
    • Mapping out the multistage fibrillation of glucagon
    • Ghodke, S. et al. Mapping out the multistage fibrillation of glucagon. FEBS J. 279, 752-765 (2012).
    • (2012) FEBS J. , vol.279 , pp. 752-765
    • Ghodke, S.1
  • 13
    • 84878709366 scopus 로고    scopus 로고
    • Non-equilibrium nature of twodimensional isotropic and nematic coexistence in amyloid fibrils at liquid interfaces
    • Jordens, S., Isa, L., Usov, I. & Mezzenga, R. Non-equilibrium nature of twodimensional isotropic and nematic coexistence in amyloid fibrils at liquid interfaces. Nat. Commun. 4, 1917 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 1917
    • Jordens, S.1    Isa, L.2    Usov, I.3    Mezzenga, R.4
  • 14
    • 70450285373 scopus 로고    scopus 로고
    • Nanocomposites: Nanoparticles in the right place
    • Mezzenga, R. & Ruokolainen, J. Nanocomposites: nanoparticles in the right place. Nat. Mater. 8, 926-928 (2009).
    • (2009) Nat. Mater. , vol.8 , pp. 926-928
    • Mezzenga, R.1    Ruokolainen, J.2
  • 15
    • 10444285330 scopus 로고    scopus 로고
    • Mechanism of the transition between lamellar and gyroid phases formed by a diblock copolymer in aqueous solution
    • Hamley, I. W. et al. Mechanism of the transition between lamellar and gyroid phases formed by a diblock copolymer in aqueous solution. Langmuir 20, 10785-10790 (2004).
    • (2004) Langmuir , vol.20 , pp. 10785-10790
    • Hamley, I.W.1
  • 16
    • 23144457209 scopus 로고    scopus 로고
    • Hierarchical self-assembly of a coiled-coil peptide into fractal structure
    • Lomander, A., Hwang, W. & Zhang, S. Hierarchical self-assembly of a coiled-coil peptide into fractal structure. Nano Lett. 5, 1255-1260 (2005).
    • (2005) Nano Lett. , vol.5 , pp. 1255-1260
    • Lomander, A.1    Hwang, W.2    Zhang, S.3
  • 17
    • 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 300, 625-627 (2003).
    • (2003) Science , vol.300 , pp. 625-627
    • Reches, M.1    Gazit, E.2
  • 18
    • 34548067360 scopus 로고    scopus 로고
    • Following the aggregation of amyloidforming peptides by computer simulations
    • Melquiond, A., Boucher, G., Mousseau, N. & Derreumaux, P. Following the aggregation of amyloidforming peptides by computer simulations. J. Chem. Phys. 122, 174904-174908 (2005).
    • (2005) J. Chem. Phys. , vol.122 , pp. 174904-174908
    • Melquiond, A.1    Boucher, G.2    Mousseau, N.3    Derreumaux, P.4
  • 19
    • 61549102795 scopus 로고    scopus 로고
    • What determines the structure and stability of KFFE monomers, dimers, and protobrils
    • Bellesia, G. & Shea, J.-E. What determines the structure and stability of KFFE monomers, dimers, and protobrils? Biophys. J. 96, 875-886 (2009).
    • (2009) Biophys. J. , vol.96 , pp. 875-886
    • Bellesia, G.1    Shea, J.-E.2
  • 20
    • 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. 39, 1877-1890 (2010).
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 1877-1890
    • Yan, X.1    Zhu, P.2    Li, J.3
  • 21
    • 77649092087 scopus 로고    scopus 로고
    • Strong piezoelectricity in bioinspired peptide nanotubes
    • Kholkin, A., Amdursky, N., Bdikin, I., Gazit, E. & Rosenman, G. Strong piezoelectricity in bioinspired peptide nanotubes. ACS Nano 4, 610-614 (2010).
    • (2010) ACS Nano , vol.4 , pp. 610-614
    • Kholkin, A.1    Amdursky, N.2    Bdikin, I.3    Gazit, E.4    Rosenman, G.5
  • 22
    • 84856498851 scopus 로고    scopus 로고
    • Evidence of ferroelectricity and phase transition in pressed diphenylalanine peptide nanotubes
    • Bdikin, I. et al. Evidence of ferroelectricity and phase transition in pressed diphenylalanine peptide nanotubes. Appl. Phys. Lett. 100, 043702-043704 (2012).
    • (2012) Appl. Phys. Lett. , vol.100 , pp. 043702-043704
    • Bdikin, I.1
  • 23
    • 70349967919 scopus 로고    scopus 로고
    • Blue luminescence based on quantum confinement at peptide nanotubes
    • Amdursky, N. et al. Blue luminescence based on quantum confinement at peptide nanotubes. Nano Lett. 9, 3111-3115 (2009).
    • (2009) Nano Lett. , vol.9 , pp. 3111-3115
    • Amdursky, N.1
  • 24
    • 84873744124 scopus 로고    scopus 로고
    • Tuning the mechanical properties of self-assembled mixed-peptide tubes
    • Sedman, V. et al. Tuning the mechanical properties of self-assembled mixed-peptide tubes. J. Microsc. 249, 165-172 (2013).
    • (2013) J. Microsc. , vol.249 , pp. 165-172
    • Sedman, V.1
  • 25
    • 34547217464 scopus 로고    scopus 로고
    • Using the bending beam model to estimate the elasticity of diphenylalanine nanotubes
    • Niu, L., Chen, X., Allen, S. & Tendler, S. J. B. Using the bending beam model to estimate the elasticity of diphenylalanine nanotubes. Langmuir 23, 7443-7446 (2007).
    • (2007) Langmuir , vol.23 , pp. 7443-7446
    • Niu, L.1    Chen, X.2    Allen, S.3    Tendler, S.J.B.4
  • 26
    • 33244497383 scopus 로고    scopus 로고
    • Thermal and chemical stability of diphenylalanine peptide nanotubes: Implications for nanotechnological applications
    • Adler-Abramovich, L. et al. Thermal and chemical stability of diphenylalanine peptide nanotubes: implications for nanotechnological applications. Langmuir 22, 1313-1320 (2006).
    • (2006) Langmuir , vol.22 , pp. 1313-1320
    • Adler-Abramovich, L.1
  • 27
    • 68649108646 scopus 로고    scopus 로고
    • Fmocdiphenylalanine self-assembly mechanism induces apparent pK(a) shifts
    • Tang, C., Smith, A. M., Collins, R. F., Ulijn, R. V. & Saiani, A. Fmocdiphenylalanine self-assembly mechanism induces apparent pK(a) shifts. Langmuir 25, 9447-9453 (2009).
    • (2009) Langmuir , vol.25 , pp. 9447-9453
    • Tang, C.1    Smith, A.M.2    Collins, R.F.3    Ulijn, R.V.4    Saiani, A.5
  • 28
    • 54949125704 scopus 로고    scopus 로고
    • High-temperature self-assembly of peptides into vertically well-aligned nanowires by aniline vapor
    • Ryu, J. & Park, C. B. High-temperature self-assembly of peptides into vertically well-aligned nanowires by aniline vapor. Adv. Mater. 20, 3754-3758 (2008).
    • (2008) Adv. Mater. , vol.20 , pp. 3754-3758
    • Ryu, J.1    Park, C.B.2
  • 29
    • 37549063068 scopus 로고    scopus 로고
    • Role of intermolecular forces in defining material properties of protein nanofibrils
    • Knowles, T. P. et al. Role of intermolecular forces in defining material properties of protein nanofibrils. Science. 318, 1900-1903 (2007).
    • (2007) Science. , vol.318 , pp. 1900-1903
    • Knowles, T.P.1
  • 30
    • 84870054457 scopus 로고    scopus 로고
    • Autonomous motors of a metalorganic framework powered by reorganization of selfassembled peptides at interfaces
    • Ikezoe, Y., Washino, G., Uemura, T., Kitagawa, S. & Matsui, H. Autonomous motors of a metalorganic framework powered by reorganization of selfassembled peptides at interfaces. Nat. Mater. 11, 1081-1085 (2012).
    • (2012) Nat. Mater. , vol.11 , pp. 1081-1085
    • Ikezoe, Y.1    Washino, G.2    Uemura, T.3    Kitagawa, S.4    Matsui, H.5
  • 31
    • 77049089028 scopus 로고    scopus 로고
    • Role of water in directing diphenylalanine assembly into nanotubes and nanowires
    • Kim, J. et al. Role of water in directing diphenylalanine assembly into nanotubes and nanowires. Adv. Mater. 22, 583-587 (2010).
    • (2010) Adv. Mater. , vol.22 , pp. 583-587
    • Kim, J.1
  • 32
    • 80155174800 scopus 로고    scopus 로고
    • Salt-induced hydrogelation of functionalised-dipeptides at high pH
    • Chen, L. et al. Salt-induced hydrogelation of functionalised-dipeptides at high pH. Chem. Commun. 47, 12071-12073 (2011).
    • (2011) Chem. Commun. , vol.47 , pp. 12071-12073
    • Chen, L.1
  • 33
    • 53849114310 scopus 로고    scopus 로고
    • Reversible transitions between peptide nanotubes and vesicle-like structures including theoretical modeling studies
    • Yan, X. et al. Reversible transitions between peptide nanotubes and vesicle-like structures including theoretical modeling studies. Chem. Eur. J. 14, 5974-5980 (2008).
    • (2008) Chem. Eur. J. , vol.14 , pp. 5974-5980
    • Yan, X.1
  • 34
    • 23344437452 scopus 로고    scopus 로고
    • Self-assembly of peptide nanotubes and amyloid-like structures by chargedtermini capped diphenylalanine peptide analogues
    • Reches, M. & Gazit, E. Self-assembly of peptide nanotubes and amyloid-like structures by chargedtermini capped diphenylalanine peptide analogues. Isr. J. Chem. 45, 363-371 (2005).
    • (2005) Isr. J. Chem. , vol.45 , pp. 363-371
    • Reches, M.1    Gazit, E.2
  • 35
    • 78650302532 scopus 로고    scopus 로고
    • Self-assembled organic nanostructures with metallic-like stiffness
    • Adler-Abramovich, L. et al. Self-assembled organic nanostructures with metallic-like stiffness. Angew. Chem. Int. Ed. 49, 9939-9942 (2010).
    • (2010) Angew. Chem. Int. Ed. , vol.49 , pp. 9939-9942
    • Adler-Abramovich, L.1
  • 36
    • 0001732841 scopus 로고
    • Studien ber die bildung und umwandlung fester krper
    • Ostwald, W. Studien ber die bildung und umwandlung fester krper. Z. Phys. Chem. 22, 289-330 (1897).
    • (1897) Z. Phys. Chem. , vol.22 , pp. 289-330
    • Ostwald, W.1
  • 37
    • 75749103386 scopus 로고    scopus 로고
    • Control of protein adsorption onto core-shell tubular and vesicular structures of diphenylalanine/parylene
    • Demirel, G., Malvadkar, N. & Demirel, M. C. Control of protein adsorption onto core-shell tubular and vesicular structures of diphenylalanine/parylene. Langmuir 26, 1460-1463 (2010).
    • (2010) Langmuir , vol.26 , pp. 1460-1463
    • Demirel, G.1    Malvadkar, N.2    Demirel, M.C.3
  • 38
    • 79958780904 scopus 로고    scopus 로고
    • Self-assembly into spheres of a hybrid diphenylalanine-porphyrin: Increased fluorescence lifetime and conserved electronic properties
    • Charalambidis, G., Kasotakis, E., Lazarides, T., Mitraki, A. & Coutsolelos, A. G. Self-assembly into spheres of a hybrid diphenylalanine-porphyrin: Increased fluorescence lifetime and conserved electronic properties. Chem. Eur. J. 17, 7213-7219 (2011).
    • (2011) Chem. Eur. J. , vol.17 , pp. 7213-7219
    • Charalambidis, G.1    Kasotakis, E.2    Lazarides, T.3    Mitraki, A.4    Coutsolelos, A.G.5
  • 39
    • 36048941372 scopus 로고    scopus 로고
    • Peptide fibrillization
    • Hamley, I. W. Peptide fibrillization. Angew. Chem. Int. Ed. 46, 8128-8147 (2007).
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 8128-8147
    • Hamley, I.W.1
  • 40
    • 0021837479 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. II. a double nucleation mechanism
    • Ferrone, F. A., Hofrichter, J. & Eaton, W. A. Kinetics of sickle hemoglobin polymerization. II. a double nucleation mechanism. J. Mol. Biol. 183, 611-631 (1985).
    • (1985) J. Mol. Biol. , vol.183 , pp. 611-631
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 41
    • 72149118250 scopus 로고    scopus 로고
    • An analytical solution to the kinetics of breakable filament assembly
    • Knowles, T. P. J. et al. An analytical solution to the kinetics of breakable filament assembly. Science 326, 1533-1537 (2009).
    • (2009) Science , vol.326 , pp. 1533-1537
    • Knowles, T.P.J.1
  • 42
    • 84878994873 scopus 로고    scopus 로고
    • Proliferation of Ab40 and Ab42 aggregates occurs through a secondary nucleation mechanism
    • Cohen, S. I. A. et al. Proliferation of Ab40 and Ab42 aggregates occurs through a secondary nucleation mechanism. Proc. Natl Acad. Sci. USA 110, 9758-9763 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 9758-9763
    • Cohen, S.I.A.1
  • 43
    • 84903696629 scopus 로고    scopus 로고
    • Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Ab40 and Ab42 peptides
    • Meisl, G. et al. Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Ab40 and Ab42 peptides. Proc. Natl Acad. Sci. USA 111, 9384-9389 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 9384-9389
    • Meisl, G.1
  • 44
    • 36849139523 scopus 로고
    • Kinetics of solidifcation of supercooled liquid mercury droplets
    • Turnbull, D. Kinetics of solidifcation of supercooled liquid mercury droplets. J. Chem. Phys. 20, 411-424 (1952).
    • (1952) J. Chem. Phys. , vol.20 , pp. 411-424
    • Turnbull, D.1
  • 45
    • 84896377600 scopus 로고    scopus 로고
    • Spatial propagation of protein polymerization
    • Cohen, S. I. A. et al. Spatial propagation of protein polymerization. Phys. Rev. Lett. 112, 98-101 (2014).
    • (2014) Phys. Rev. Lett. , vol.112 , pp. 98-101
    • Cohen, S.I.A.1
  • 46
    • 80052607718 scopus 로고    scopus 로고
    • Observation of spatial propagation of amyloid assembly from single nuclei
    • Knowles, T. P. J. et al. Observation of spatial propagation of amyloid assembly from single nuclei. Proc. Natl Acad. Sci. USA. 108, 14746-14751 (2011).
    • (2011) Proc. Natl Acad. Sci. USA. , vol.108 , pp. 14746-14751
    • Knowles, T.P.J.1
  • 47
    • 33646109512 scopus 로고
    • The kinetics of precipitation from supersaturated solid solutions
    • Lifshitz, I. & Slyozov, V. The kinetics of precipitation from supersaturated solid solutions. J. Phys. Chem. Solids 19, 35-50 (1961).
    • (1961) J. Phys. Chem. Solids , vol.19 , pp. 35-50
    • Lifshitz, I.1    Slyozov, V.2
  • 48
    • 33751291121 scopus 로고
    • Ostwald ripening of precipitates
    • Kahlweit, M. Ostwald ripening of precipitates. Adv. Colloid Interface Sci. 5, 1-35 (1975).
    • (1975) Adv. Colloid Interface Sci. , vol.5 , pp. 1-35
    • Kahlweit, M.1
  • 49
    • 0001333772 scopus 로고
    • Theorie der alterung von niederschlgen durch umlsen (ostwald-reifung)
    • Wagner, C. Theorie der alterung von niederschlgen durch umlsen (ostwald-reifung). Ber. Bunsenges. Phys. Chem. 65, 581-591 (1961).
    • (1961) Ber. Bunsenges. Phys. Chem. , vol.65 , pp. 581-591
    • Wagner, C.1
  • 50
    • 0020141080 scopus 로고
    • On the ostwald ripening theory, overview 20
    • Vengrenovich, R. D. On the ostwald ripening theory, overview 20. Acta Metall. 20, 1079-1086 (1982).
    • (1982) Acta Metall. , vol.20 , pp. 1079-1086
    • Vengrenovich, R.D.1
  • 51
    • 34249781400 scopus 로고    scopus 로고
    • Ostwald ripening: A synthetic approach for hollow nanomaterials
    • Zeng, H. C. Ostwald ripening: a synthetic approach for hollow nanomaterials. Curr. Nanosci. 3, 177-181 (2007).
    • (2007) Curr. Nanosci. , vol.3 , pp. 177-181
    • Zeng, H.C.1
  • 52
    • 0000393948 scopus 로고    scopus 로고
    • Growth kinetics of nanocrystalline ZnO particles from colloidal suspensions
    • Wong, E. M., Bonevich, J. E. & Searson, P. C. Growth kinetics of nanocrystalline ZnO particles from colloidal suspensions. J. Phys. Chem. B 102, 7770-7775 (1998).
    • (1998) J. Phys. Chem. B , vol.102 , pp. 7770-7775
    • Wong, E.M.1    Bonevich, J.E.2    Searson, P.C.3
  • 53
    • 0032654646 scopus 로고    scopus 로고
    • Selection of suitable dispersants for aqueous suspensions of zirconia and titania powders using acoustophoresis
    • Greenwood, R. & Kendall, K. Selection of suitable dispersants for aqueous suspensions of zirconia and titania powders using acoustophoresis. J. Eur. Ceram. Soc. 19, 479-488 (1999).
    • (1999) J. Eur. Ceram. Soc. , vol.19 , pp. 479-488
    • Greenwood, R.1    Kendall, K.2
  • 54
    • 1642304641 scopus 로고    scopus 로고
    • Preparation of hollow anatase TiO2 nanospheres via ostwald ripening
    • Yang, H. G. & Zeng, H. C. Preparation of hollow anatase TiO2 nanospheres via ostwald ripening. J. Phys. Chem. B 108, 3492-3495 (2004).
    • (2004) J. Phys. Chem. B , vol.108 , pp. 3492-3495
    • Yang, H.G.1    Zeng, H.C.2
  • 55
    • 58149269246 scopus 로고    scopus 로고
    • Multiphase transformation and ostwald's rule of stages during crystallization of a metal phosphate
    • Chung, S.-Y., Kim, Y.-M., Kim, J.-G. & Kim, Y.-J. Multiphase transformation and ostwald's rule of stages during crystallization of a metal phosphate. Nat. Phys. 5, 68-73 (2009).
    • (2009) Nat. Phys. , vol.5 , pp. 68-73
    • Chung, S.-Y.1    Kim, Y.-M.2    Kim, J.-G.3    Kim, Y.-J.4
  • 57
    • 57149102288 scopus 로고    scopus 로고
    • A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates
    • Auer, S., Meersman, F., Dobson, C. M. & Vendruscolo, M. A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates. PLoS Comput. Biol. 4, e1000222 (2008).
    • (2008) PLoS Comput. Biol. , vol.4 , pp. e1000222
    • Auer, S.1    Meersman, F.2    Dobson, C.M.3    Vendruscolo, M.4
  • 58
    • 82655189153 scopus 로고    scopus 로고
    • Size-dependent growth of polymorphs in nanopores and ostwald's step rule of stages
    • Rengarajan, G. T., Enke, D., Steinhart, M. & Beiner, M. Size-dependent growth of polymorphs in nanopores and ostwald's step rule of stages. Phys. Chem. Chem. Phys. 13, 21367-21374 (2011).
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 21367-21374
    • Rengarajan, G.T.1    Enke, D.2    Steinhart, M.3    Beiner, M.4
  • 59
    • 84887040270 scopus 로고    scopus 로고
    • Kinetically controlled self-assembly of redox-active ferrocene-diphenylalanine: From nanospheres to nanofibers
    • Wang, Y. et al. Kinetically controlled self-assembly of redox-active ferrocene-diphenylalanine: from nanospheres to nanofibers. Nanotechnology 24, 465603 (2013).
    • (2013) Nanotechnology , vol.24 , pp. 465603
    • Wang, Y.1
  • 60
    • 84894627201 scopus 로고    scopus 로고
    • Expanding the solvent chemical space for self-assembly of dipeptide nanostructures
    • Mason, T. O. et al. Expanding the solvent chemical space for self-assembly of dipeptide nanostructures. ACS Nano 8, 1243-1253 (2014).
    • (2014) ACS Nano , vol.8 , pp. 1243-1253
    • Mason, T.O.1
  • 61
    • 79953729372 scopus 로고    scopus 로고
    • Formation of single-walled aluminosilicate nanotubes from molecular precursors and curved nanoscale intermediates
    • Yucelen, G. I. et al. Formation of single-walled aluminosilicate nanotubes from molecular precursors and curved nanoscale intermediates. J. Am. Chem. Soc. 133, 5397-5412 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 5397-5412
    • Yucelen, G.I.1
  • 62
    • 84872864833 scopus 로고    scopus 로고
    • A generalized kinetic model for the formation and growth of single-walled metal oxide nanotubes
    • Yucelen, G. I., Kang, D.-Y., Schmidt-Krey, I., Beckham, H. W. & Nair, S. A generalized kinetic model for the formation and growth of single-walled metal oxide nanotubes. Chem. Eng. Sci. 90, 200-212 (2013).
    • (2013) Chem. Eng. Sci. , vol.90 , pp. 200-212
    • Yucelen, G.I.1    Kang, D.-Y.2    Schmidt-Krey, I.3    Beckham, H.W.4    Nair, S.5
  • 63
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of a-Synuclein
    • Cremades, N. et al. Direct observation of the interconversion of normal and toxic forms of a-Synuclein. Cell 149, 1048-1059 (2012).
    • (2012) Cell , vol.149 , pp. 1048-1059
    • Cremades, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.