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Volumn 12, Issue 9, 2011, Pages 5736-5746

Ultrasmall peptides self-assemble into diverse nanostructures: Morphological evaluation and potential implications anupama

Author keywords

Bioengineering; Nanotechnology; Origin of life; Self assembly; Supramolecular structures; Ultrasmall peptides

Indexed keywords

AROMATIC AMINO ACID; NANOMATERIAL; PEPTIDE; PEPTIDE NANOTUBE;

EID: 80053200885     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms12095736     Document Type: Article
Times cited : (31)

References (31)
  • 1
    • 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
  • 2
    • 1542276719 scopus 로고    scopus 로고
    • Molecular Self-Assembly and the Origin of Life
    • 1st ed.; Horneck, G., Baumstark-Khan, C., Eds.; Springer: Berlin, Germany
    • Heckl, W.M. Molecular Self-Assembly and the Origin of Life. In Astrobiology the Quest for the Conditions of Life, 1st ed.; Horneck, G., Baumstark-Khan, C., Eds.; Springer: Berlin, Germany, 2002; pp. 360-371.
    • (2002) Astrobiology the Quest For the Conditions of Life , pp. 360-371
    • Heckl, W.M.1
  • 3
    • 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
  • 5
    • 77954946648 scopus 로고    scopus 로고
    • Designer self-assembling peptide nanofiber biological materials
    • Hauser, C.A.E.; Zhang, S. Designer self-assembling peptide nanofiber biological materials. Chem. Soc. Rev. 2010, 39, 2780-2790.
    • (2010) Chem. Soc. Rev , vol.39 , pp. 2780-2790
    • Hauser, C.A.E.1    Zhang, S.2
  • 7
    • 0035941074 scopus 로고    scopus 로고
    • Self-assembly and mineralization of peptide-amphiphile nanofibers
    • Hartgerink, J.D.; Beniash, E.; Stupp, S.I. Self-assembly and mineralization of peptide-amphiphile nanofibers. Science 2001, 294, 1684-1688.
    • (2001) Science , vol.294 , pp. 1684-1688
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 8
    • 0037117535 scopus 로고    scopus 로고
    • Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles
    • Vauthey, S.; Santoso, S.; Gong, H.; Watson, N.; Zhang, S. Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles. Proc. Natl. Acad. Sci. USA 2002, 99, 5355-5360.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5355-5360
    • Vauthey, S.1    Santoso, S.2    Gong, H.3    Watson, N.4    Zhang, S.5
  • 9
    • 0033740122 scopus 로고    scopus 로고
    • Modulated supramolecular assemblies composed of tripeptide derivatives: Formation of micrometer-scale rods, nanometer-size needles, and regular patterns with molecular-level flatness from the same compound
    • Ariga, K.; Kikuchi, J.; Naito, M.; Koyama, E.; Yamada, N. Modulated supramolecular assemblies composed of tripeptide derivatives: formation of micrometer-scale rods, nanometer-size needles, and regular patterns with molecular-level flatness from the same compound. Langmuir 2000, 16, 4929-4939.
    • (2000) Langmuir , vol.16 , pp. 4929-4939
    • Ariga, K.1    Kikuchi, J.2    Naito, M.3    Koyama, E.4    Yamada, N.5
  • 10
    • 66249146049 scopus 로고    scopus 로고
    • Complexity in Biomaterials for Tissue Engineering
    • Place, E.S.; Evans, N.D.; Stevens, M.M. Complexity in Biomaterials for Tissue Engineering. Nat. Mater. 2009, 8, 457-470.
    • (2009) Nat. Mater , vol.8 , pp. 457-470
    • Place, E.S.1    Evans, N.D.2    Stevens, M.M.3
  • 11
    • 33244497383 scopus 로고    scopus 로고
    • Thermal and chemical stability of diphenylalanine peptide nanotubes: Implications for nanotechnological applications
    • Adler-Abramovich, L.; Reches, M.; Sedman, V.L.; Allen, S.; Tendler, S.J.B.; Gazit, E. Thermal and chemical stability of diphenylalanine peptide nanotubes: Implications for nanotechnological applications. Langmuir 2006, 22, 1313-1320.
    • (2006) Langmuir , vol.22 , pp. 1313-1320
    • Adler-Abramovich, L.1    Reches, M.2    Sedman, V.L.3    Allen, S.4    Tendler, S.J.B.5    Gazit, E.6
  • 13
    • 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
  • 14
    • 33947369859 scopus 로고    scopus 로고
    • Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology
    • Marek, P.; Abedini, A.; Song, B.; Kanungo, M.; Johnson, M.E.; Gupta, R.; Zaman, W.; Wong, S.S.; Raleigh, D.P. Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology. Biochemistry 2007, 46, 3255-3261.
    • (2007) Biochemistry , vol.46 , pp. 3255-3261
    • Marek, P.1    Abedini, A.2    Song, B.3    Kanungo, M.4    Johnson, M.E.5    Gupta, R.6    Zaman, W.7    Wong, S.S.8    Raleigh, D.P.9
  • 15
    • 80053191302 scopus 로고
    • The Origin of Life; Macmillan: New York, NY, USA
    • Oparin, A.I. The Origin of Life; Macmillan: New York, NY, USA, 1938.
    • (1938)
    • Oparin, A.I.1
  • 16
    • 37049243502 scopus 로고
    • A production of amino acids under possible primitive earth conditions
    • Miller, S.L. A production of amino acids under possible primitive earth conditions. Science 1953, 117, 528-529.
    • (1953) Science , vol.117 , pp. 528-529
    • Miller, S.L.1
  • 17
    • 0032768196 scopus 로고    scopus 로고
    • Peptides and the origin of life
    • Rode, B.M. Peptides and the origin of life. Peptides 1999, 20, 773-786.
    • (1999) Peptides , vol.20 , pp. 773-786
    • Rode, B.M.1
  • 18
    • 38049048820 scopus 로고    scopus 로고
    • The first steps of chemical evolution towards the origin of life
    • Rode, B.M.; Fitz, D.; Jakschitz, T. The first steps of chemical evolution towards the origin of life. Chem. Biodivers. 2007, 4, 2674-2702.
    • (2007) Chem. Biodivers , vol.4 , pp. 2674-2702
    • Rode, B.M.1    Fitz, D.2    Jakschitz, T.3
  • 19
    • 0027031301 scopus 로고
    • Investigations on the mechanism of the salt-induced peptide formation
    • Schwendinger, M.G.; Rode, B.M. Investigations on the mechanism of the salt-induced peptide formation. Orig. Life Evol. Biosph. 1992, 22, 349-359.
    • (1992) Orig. Life Evol. Biosph , vol.22 , pp. 349-359
    • Schwendinger, M.G.1    Rode, B.M.2
  • 20
    • 14844303886 scopus 로고    scopus 로고
    • Single turn peptide alpha helices with exceptional stability in water
    • Shepherd, N.E.; Hoang, H.N.; Abbenante, G.; Fairlie, D.P. Single turn peptide alpha helices with exceptional stability in water. J. Am. Chem. Soc. 2005, 127, 2974-2983.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 2974-2983
    • Shepherd, N.E.1    Hoang, H.N.2    Abbenante, G.3    Fairlie, D.P.4
  • 22
    • 0037162463 scopus 로고    scopus 로고
    • Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: Implications for cartilage tissue repair
    • Kisiday, J.; Jin, M.; Kurz, B.; Hung, H.; Semino, C.; Zhang, S.; Grodzinsky, A.J. Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: implications for cartilage tissue repair. Proc. Natl. Acad. Sci. USA 2002, 99, 9996-10001.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9996-10001
    • Kisiday, J.1    Jin, M.2    Kurz, B.3    Hung, H.4    Semino, C.5    Zhang, S.6    Grodzinsky, A.J.7
  • 23
    • 77957703908 scopus 로고    scopus 로고
    • Functionalized scaffolds of shorter self-assembling peptides containing MMP-2 cleavable motif promote fibroblast proliferation and significantly accelerate 3-D cell migration independent of scaffold stiffness
    • Kumada, Y.; Hammond, N.A.; Zhang, S. Functionalized scaffolds of shorter self-assembling peptides containing MMP-2 cleavable motif promote fibroblast proliferation and significantly accelerate 3-D cell migration independent of scaffold stiffness. Soft Matter 2010, 6, 5073-5079.
    • (2010) Soft Matter , vol.6 , pp. 5073-5079
    • Kumada, Y.1    Hammond, N.A.2    Zhang, S.3
  • 25
    • 0035823520 scopus 로고    scopus 로고
    • Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation
    • Azriel, R.; Gazit, E. Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation. J. Biol. Chem. 2001, 276, 34156-34161.
    • (2001) J. Biol. Chem , vol.276 , pp. 34156-34161
    • Azriel, R.1    Gazit, E.2
  • 26
    • 33744932979 scopus 로고    scopus 로고
    • The Structure of nanotubes formed by diphenylalanine, the core recognition motif of Alzheimer's β-amyloid polypeptide
    • Gorbitz, C.H. The Structure of nanotubes formed by diphenylalanine, the core recognition motif of Alzheimer's β-amyloid polypeptide. Chem. Commun. 2006, 2332-2334.
    • (2006) Chem. Commun , pp. 2332-2334
    • Gorbitz, C.H.1
  • 27
    • 0036135139 scopus 로고    scopus 로고
    • Possible role for π-Stacking in the self-assembly of amyloid fibrils
    • Gazit, E.A. Possible role for π-Stacking in the self-assembly of amyloid fibrils. FASEB J. 2002, 16, 77-83.
    • (2002) FASEB J , vol.16 , pp. 77-83
    • Gazit, E.A.1
  • 28
    • 33645510751 scopus 로고    scopus 로고
    • Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase
    • Bemporad, F.; Taddei, N.; Stefani, M.; Chiti, F. Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase. Protein Sci. 2006, 15, 862-870.
    • (2006) Protein Sci , vol.15 , pp. 862-870
    • Bemporad, F.1    Taddei, N.2    Stefani, M.3    Chiti, F.4
  • 29
    • 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
  • 30
    • 12844264701 scopus 로고    scopus 로고
    • Novel electrochemical biosensing platform using self-assembled peptide nanotubes
    • Yemini, M.; Reches, M.; Rishpon, J.; Gazit, E. Novel electrochemical biosensing platform using self-assembled peptide nanotubes. Nano Lett. 2004, 5, 183-186.
    • (2004) Nano Lett , vol.5 , pp. 183-186
    • Yemini, M.1    Reches, M.2    Rishpon, J.3    Gazit, E.4
  • 31
    • 23744509819 scopus 로고    scopus 로고
    • Peptide nanotube-modified electrodes for enzyme-biosensor applications
    • Yemini, M.; Reches, M.; Gazit, E.; Rishpon, J. Peptide nanotube-modified electrodes for enzyme-biosensor applications. Anal. Chem. 2005, 77, 5155-5159.
    • (2005) Anal. Chem , vol.77 , pp. 5155-5159
    • Yemini, M.1    Reches, M.2    Gazit, E.3    Rishpon, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.