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Volumn 18, Issue 5, 2012, Pages 283-292

Self-assembly of short peptides composed of only aliphatic amino acids and a combination of aromatic and aliphatic amino acids

Author keywords

Beta structure; Hydrophobic peptides; Nanotubes; Self assembly; Spherical nanostructures

Indexed keywords

ALIPHATIC AMINO ACID; AMINO ACID; AROMATIC AMINO ACID; METHANOL; NANOTUBE; UNCLASSIFIED DRUG;

EID: 84859641418     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.2395     Document Type: Article
Times cited : (24)

References (63)
  • 2
    • 60849117286 scopus 로고    scopus 로고
    • Organic solvent mediated self-association of an amyloid forming peptide from beta2-microglobulin: an atomic force microscopy study
    • Chaudhary N, Singh S, Nagaraj R. Organic solvent mediated self-association of an amyloid forming peptide from beta2-microglobulin: an atomic force microscopy study. Biopolymers 2008; 90: 783-791.
    • (2008) Biopolymers , vol.90 , pp. 783-791
    • Chaudhary, N.1    Singh, S.2    Nagaraj, R.3
  • 3
    • 70449721154 scopus 로고    scopus 로고
    • Morphology of self-assembled structures formed by short peptides from the amyloidogenic protein tau depends on the solvent in which the peptides are dissolved
    • Chaudhary N, Singh S, Nagaraj R. Morphology of self-assembled structures formed by short peptides from the amyloidogenic protein tau depends on the solvent in which the peptides are dissolved. J. Pept. Sci. 2009; 15: 675-684.
    • (2009) J. Pept. Sci. , vol.15 , pp. 675-684
    • Chaudhary, N.1    Singh, S.2    Nagaraj, R.3
  • 4
    • 36048941372 scopus 로고    scopus 로고
    • Peptide fibrillization
    • Hamley IW. Peptide fibrillization. Angew. Chem. Int. Ed. 2007; 46: 8128-8147.
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 8128-8147
    • Hamley, I.W.1
  • 5
    • 33845637320 scopus 로고    scopus 로고
    • From the polymorphism of amyloid fibrils to their assembly mechanism and cytotoxicity
    • Kreplak L, Aebi U. From the polymorphism of amyloid fibrils to their assembly mechanism and cytotoxicity. Adv. Protein Chem. 2006; 73: 217-233.
    • (2006) Adv. Protein Chem. , vol.73 , pp. 217-233
    • Kreplak, L.1    Aebi, U.2
  • 7
    • 33750084721 scopus 로고    scopus 로고
    • Aggregation of the amphipathic peptides (AAKA)n into antiparallel β-sheets
    • Measey TJ, Schweitzer-Stenner R. Aggregation of the amphipathic peptides (AAKA)n into antiparallel β-sheets. J. Am. Chem. Soc. 2006; 128: 13324-13325.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 13324-13325
    • Measey, T.J.1    Schweitzer-Stenner, R.2
  • 8
  • 10
    • 37549031260 scopus 로고    scopus 로고
    • Amyloid-a state in many guises: survival of the fittest fibril fold
    • Pedersen JS, Otzen DE. Amyloid-a state in many guises: survival of the fittest fibril fold. Protein Sci. 2008; 17: 2-10.
    • (2008) Protein Sci. , vol.17 , pp. 2-10
    • Pedersen, J.S.1    Otzen, D.E.2
  • 13
    • 48449106540 scopus 로고    scopus 로고
    • Electrochemical devices made from conducting nanowire networks self-assembled from amyloid fibrils and alkoxysulfonate PEDOT
    • Hamedi M, Herland A, Karlsson RH, Inganas O. Electrochemical devices made from conducting nanowire networks self-assembled from amyloid fibrils and alkoxysulfonate PEDOT. Nano Lett. 2008; 8: 1736-1740.
    • (2008) Nano Lett. , vol.8 , pp. 1736-1740
    • Hamedi, M.1    Herland, A.2    Karlsson, R.H.3    Inganas, O.4
  • 14
    • 33751516396 scopus 로고    scopus 로고
    • Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure
    • Sokolov Y, Kozak JA, Kayed R, Chanturiya A, Glabe C, Hall JE. Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure. J. Gen. Physiol. 2006; 128: 637-647.
    • (2006) J. Gen. Physiol. , vol.128 , pp. 637-647
    • Sokolov, Y.1    Kozak, J.A.2    Kayed, R.3    Chanturiya, A.4    Glabe, C.5    Hall, J.E.6
  • 16
    • 0035941074 scopus 로고    scopus 로고
    • Self-assembly and mineralization of peptide-amphiphile nanofibers
    • Hartgerink JD, Beniash E, Stupp SI. 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
  • 17
    • 67549083305 scopus 로고    scopus 로고
    • Production of self-assembling biomaterials for tissue engineering
    • Kyle S, Aggeli A, Ingham E, McPherson MJ. Production of self-assembling biomaterials for tissue engineering. Trends Biotechnol. 2009; 27: 423-433.
    • (2009) Trends Biotechnol. , vol.27 , pp. 423-433
    • Kyle, S.1    Aggeli, A.2    Ingham, E.3    McPherson, M.J.4
  • 19
    • 37849047811 scopus 로고    scopus 로고
    • Molecular self-assembly bioactive nanostructures branch out
    • Gazit E. Molecular self-assembly bioactive nanostructures branch out. Nat. Nanotechnol. 2008; 3: 8-9.
    • (2008) Nat. Nanotechnol. , vol.3 , pp. 8-9
    • Gazit, E.1
  • 20
    • 69949150597 scopus 로고    scopus 로고
    • Controlled release from modified amino acid hydrogels governed by molecular size or network dynamics
    • Sutton S, Campbell NL, Cooper AI, Kirkland M, Frith WJ, Adams DJ. Controlled release from modified amino acid hydrogels governed by molecular size or network dynamics. Langmuir 2009; 25: 10285-10291.
    • (2009) Langmuir , vol.25 , pp. 10285-10291
    • Sutton, S.1    Campbell, N.L.2    Cooper, A.I.3    Kirkland, M.4    Frith, W.J.5    Adams, D.J.6
  • 23
    • 0035802949 scopus 로고    scopus 로고
    • Nanotube formation by hydrophobic dipeptides
    • Görbitz CH. Nanotube formation by hydrophobic dipeptides. Chem. Eur. J. 2001; 7: 5153-5159.
    • (2001) Chem. Eur. J. , vol.7 , pp. 5153-5159
    • Görbitz, C.H.1
  • 26
    • 2342595738 scopus 로고    scopus 로고
    • Formation of closed-cage nanostructures by self-assembly of aromatic dipeptides
    • Reches M, Gazit E. Formation of closed-cage nanostructures by self-assembly of aromatic dipeptides. Nano Lett. 2004; 4: 581-585.
    • (2004) Nano Lett. , vol.4 , pp. 581-585
    • Reches, M.1    Gazit, E.2
  • 27
    • 44649172609 scopus 로고    scopus 로고
    • Self-assembling peptide nanotubes
    • Scanlon S, Amalia A. Self-assembling peptide nanotubes. Nano Today 2008; 3: 22-30.
    • (2008) Nano Today , vol.3 , pp. 22-30
    • Scanlon, S.1    Amalia, A.2
  • 28
    • 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. U. S. A. 2002; 99: 5355-5360.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 5355-5360
    • Vauthey, S.1    Santoso, S.2    Gong, H.3    Watson, N.4    Zhang, S.5
  • 29
    • 78149241540 scopus 로고    scopus 로고
    • Elementary building blocks of self-assembled peptide nanotubes
    • Amdursky N, Molotskii M, Gazit E, Rosenman G. Elementary building blocks of self-assembled peptide nanotubes. J. Am. Chem. Soc. 2010; 132: 15632-15636.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15632-15636
    • Amdursky, N.1    Molotskii, M.2    Gazit, E.3    Rosenman, G.4
  • 30
    • 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
  • 32
    • 33745152345 scopus 로고    scopus 로고
    • Rigid, self-assembled hydrogel composed of a modified aromatic dipeptide
    • Mahler A, Reches M, Rechter M, Cohen S, Gazit E. Rigid, self-assembled hydrogel composed of a modified aromatic dipeptide. Adv. Mater. 2006; 18: 1365-1370.
    • (2006) Adv. Mater. , vol.18 , pp. 1365-1370
    • Mahler, A.1    Reches, M.2    Rechter, M.3    Cohen, S.4    Gazit, E.5
  • 33
    • 33644913129 scopus 로고    scopus 로고
    • Nanostructured hydrogels for three-dimensional cell culture through self-assembly of fluorenylmethoxycarbonyl-dipeptides
    • Jayawarna V, Ali M, Jowitt TA, Miller AF, Saiani A, Gough JE, Ulijn RV. Nanostructured hydrogels for three-dimensional cell culture through self-assembly of fluorenylmethoxycarbonyl-dipeptides. Adv. Mater. 2006; 18: 611-614.
    • (2006) Adv. Mater. , vol.18 , pp. 611-614
    • Jayawarna, V.1    Ali, M.2    Jowitt, T.A.3    Miller, A.F.4    Saiani, A.5    Gough, J.E.6    Ulijn, R.V.7
  • 34
    • 0037117523 scopus 로고    scopus 로고
    • Infinite pleated β-sheet formed by the β-hairpin Boc-β-Phe-β-Phe-d-Pro-Gly-β-Phe-β-Phe-OMe
    • Karle I, Gopi HN, Balaram P. Infinite pleated β-sheet formed by the β-hairpin Boc-β-Phe-β-Phe-d-Pro-Gly-β-Phe-β-Phe-OMe. Proc. Natl. Acad. Sci. U. S. A. 2002; 99: 5160-5164.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 5160-5164
    • Karle, I.1    Gopi, H.N.2    Balaram, P.3
  • 35
    • 65349180766 scopus 로고    scopus 로고
    • A new method for maintaining homogeneity during liquid-hydrogel transitions using low molecular weight hydrogelators
    • Adams DJ, Butler MF, Frith WJ, Mark K, Leanne M, Paul S. A new method for maintaining homogeneity during liquid-hydrogel transitions using low molecular weight hydrogelators. Soft Matter 2009; 5: 1856-1862.
    • (2009) Soft Matter , vol.5 , pp. 1856-1862
    • Adams, D.J.1    Butler, M.F.2    Frith, W.J.3    Mark, K.4    Leanne, M.5    Paul, S.6
  • 36
    • 77950590085 scopus 로고    scopus 로고
    • Hydrogelation through self-assembly of Fmoc-peptide functionalized cationic amphiphiles: potent antibacterial agent
    • Debnath S, Shome A, Das D, Das PK. Hydrogelation through self-assembly of Fmoc-peptide functionalized cationic amphiphiles: potent antibacterial agent. J. Phys. Chem. B 2010; 114: 4407-4415.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4407-4415
    • Debnath, S.1    Shome, A.2    Das, D.3    Das, P.K.4
  • 39
    • 33846593451 scopus 로고    scopus 로고
    • Microporous organic materials from hydrophobic dipeptides
    • Görbitz C. Microporous organic materials from hydrophobic dipeptides. Chem. Eur. J. 2007; 13: 1022-1031.
    • (2007) Chem. Eur. J. , vol.13 , pp. 1022-1031
    • Görbitz, C.1
  • 40
    • 77950591477 scopus 로고    scopus 로고
    • Hydrogelation and self-assembly of Fmoc-tripeptides: unexpected influence of sequence on self-assembled fibril structure, and hydrogel modulus and anisotropy
    • Cheng G, Castelletto V, Moulton CM, Newby GE, Hamley IW. Hydrogelation and self-assembly of Fmoc-tripeptides: unexpected influence of sequence on self-assembled fibril structure, and hydrogel modulus and anisotropy. Langmuir 2010; 26: 4990-4998.
    • (2010) Langmuir , vol.26 , pp. 4990-4998
    • Cheng, G.1    Castelletto, V.2    Moulton, C.M.3    Newby, G.E.4    Hamley, I.W.5
  • 41
    • 0023086320 scopus 로고
    • Circular dichroism studies on a synthetic peptide corresponding to the membrane-spanning region of vesicular stomatitis virus G protein and its fatty acyl derivative
    • Joseph M, Nagaraj R. Circular dichroism studies on a synthetic peptide corresponding to the membrane-spanning region of vesicular stomatitis virus G protein and its fatty acyl derivative. Biochim. Biophys. Acta 1987; 911 231-237.
    • (1987) Biochim. Biophys. Acta , vol.911 , pp. 231-237
    • Joseph, M.1    Nagaraj, R.2
  • 42
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins
    • Chou PY, Fasman GD. Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins. Biochemistry 1974; 13: 211-222.
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 43
    • 67650799934 scopus 로고    scopus 로고
    • Influence of the solvent on the self-assembly of a modified amyloid beta peptide fragment. I. Morphological investigation
    • Castelletto V, Hamley IW, Harris PJF, Olsson U, Spencer N. Influence of the solvent on the self-assembly of a modified amyloid beta peptide fragment. I. Morphological investigation. J. Phys. Chem. B 2009; 113: 9978-9987.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 9978-9987
    • Castelletto, V.1    Hamley, I.W.2    Harris, P.J.F.3    Olsson, U.4    Spencer, N.5
  • 45
    • 35348898324 scopus 로고    scopus 로고
    • Fibrillisation in organic solvent of a hydrophobically modified amyloid peptide fragment
    • Krysmann MJ, Castelletto V, Hamley IW. Fibrillisation in organic solvent of a hydrophobically modified amyloid peptide fragment. Soft Matter 2007; 3: 1401-1406.
    • (2007) Soft Matter , vol.3 , pp. 1401-1406
    • Krysmann, M.J.1    Castelletto, V.2    Hamley, I.W.3
  • 47
    • 34247243833 scopus 로고    scopus 로고
    • Controlled patterning of aligned self-assembled peptide nanotubes
    • Reches M, Gazit E. Controlled patterning of aligned self-assembled peptide nanotubes. Nat. Nanotechnol. 2006; 1: 195-200.
    • (2006) Nat. Nanotechnol. , vol.1 , pp. 195-200
    • Reches, M.1    Gazit, E.2
  • 48
    • 0027241814 scopus 로고
    • Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease
    • Fink AL, Calciano LJ, Goto Y, Nishimura M, Swedberg SA. Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease. Protein Sci. 1993; 2: 1155-1160.
    • (1993) Protein Sci. , vol.2 , pp. 1155-1160
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Nishimura, M.4    Swedberg, S.A.5
  • 49
    • 0035804936 scopus 로고    scopus 로고
    • Identification of a novel human islet amyloid polypeptide [beta]-sheet domain and factors influencing fibrillogenesis
    • Jaikaran ETAS, Higham CE, Serpell LC, Zurdo J, Gross M, Clark A, Fraser PE. Identification of a novel human islet amyloid polypeptide [beta]-sheet domain and factors influencing fibrillogenesis. J. Mol. Biol. 2001; 308: 515-525.
    • (2001) J. Mol. Biol. , vol.308 , pp. 515-525
    • Jaikaran, E.T.A.S.1    Higham, C.E.2    Serpell, L.C.3    Zurdo, J.4    Gross, M.5    Clark, A.6    Fraser, P.E.7
  • 50
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment
    • Surewicz WK, Mantsch HH, Chapman D. Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry 1993; 32: 389-394.
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 51
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils
    • Zandomeneghi G, Mark RHK, Margaret GM, Marcus F. FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils. Protein Sci. 2004; 13: 3314-3321.
    • (2004) Protein Sci. , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Mark, R.H.K.2    Margaret, G.M.3    Marcus, F.4
  • 52
    • 53149153117 scopus 로고    scopus 로고
    • Self-assembly in aqueous solution of a modified amyloid beta peptide fragment
    • Castelletto V, Hamley IW, Harris PJF. Self-assembly in aqueous solution of a modified amyloid beta peptide fragment. Biophys. Chem. 2008; 138: 29-35.
    • (2008) Biophys. Chem. , vol.138 , pp. 29-35
    • Castelletto, V.1    Hamley, I.W.2    Harris, P.J.F.3
  • 53
    • 0029002812 scopus 로고
    • The conformational analysis of peptides using Fourier transform IR spectroscopy
    • Haris PI, Chapman D. The conformational analysis of peptides using Fourier transform IR spectroscopy. Biopolymers 1995; 37: 251-263.
    • (1995) Biopolymers , vol.37 , pp. 251-263
    • Haris, P.I.1    Chapman, D.2
  • 54
    • 0035933540 scopus 로고    scopus 로고
    • Amyloid-like fibrils from an 18-residue peptide analogue of a part of the central domain of the B-family of silkmoth chorion proteins
    • Iconomidou VA, Chryssikos GD, Gionis V, Vriend G, Hoenger A, Hamodrakas SJ. Amyloid-like fibrils from an 18-residue peptide analogue of a part of the central domain of the B-family of silkmoth chorion proteins. FEBS Lett. 2001; 499: 268-273.
    • (2001) FEBS Lett. , vol.499 , pp. 268-273
    • Iconomidou, V.A.1    Chryssikos, G.D.2    Gionis, V.3    Vriend, G.4    Hoenger, A.5    Hamodrakas, S.J.6
  • 55
    • 0034650323 scopus 로고    scopus 로고
    • Spectroscopic methods for analysis of protein secondary structure
    • Pelton JT, McLean LR. Spectroscopic methods for analysis of protein secondary structure. Anal. Biochem. 2000; 277: 167-176.
    • (2000) Anal. Biochem. , vol.277 , pp. 167-176
    • Pelton, J.T.1    McLean, L.R.2
  • 56
    • 0000591955 scopus 로고
    • Vibrational analysis of peptides, polypeptides, and proteins: characteristic amide bands of beta-turns
    • Bandekar J, Krimm S. Vibrational analysis of peptides, polypeptides, and proteins: characteristic amide bands of beta-turns. Proc. Natl. Acad. Sci. U. S. A. 1979; 76: 774-777.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 774-777
    • Bandekar, J.1    Krimm, S.2
  • 57
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm S, Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 1986; 38: 181-364.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 58
    • 78651418532 scopus 로고    scopus 로고
    • Impact on the replacement of Phe by Trp in a short fragment of Aβ amyloid peptide on the formation of fibrils
    • Chaudhary N, Nagaraj R. Impact on the replacement of Phe by Trp in a short fragment of Aβ amyloid peptide on the formation of fibrils. J. Pept. Sci. 2011; 17: 115-123.
    • (2011) J. Pept. Sci. , vol.17 , pp. 115-123
    • Chaudhary, N.1    Nagaraj, R.2
  • 59
    • 0033578401 scopus 로고    scopus 로고
    • Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins: circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor
    • Sreerama N, Manning MC, Powers ME, Zhang J-X, Goldenberg DP, Woody RW. Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins: circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor. Biochemistry 1999; 38: 10814-10822.
    • (1999) Biochemistry , vol.38 , pp. 10814-10822
    • Sreerama, N.1    Manning, M.C.2    Powers, M.E.3    Zhang, J.-X.4    Goldenberg, D.P.5    Woody, R.W.6
  • 60
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody RW. Circular dichroism. Methods Enzymol. 1995; 246: 34-71.
    • (1995) Methods Enzymol. , vol.246 , pp. 34-71
    • Woody, R.W.1
  • 61
    • 0032104620 scopus 로고    scopus 로고
    • Resolution of Trp near UV CD spectra of calmodulin-domain peptide complexes into the 1La and 1Lb component spectra
    • Barth A, Martin SR, Bayley PM. Resolution of Trp near UV CD spectra of calmodulin-domain peptide complexes into the 1La and 1Lb component spectra. Biopolymers 1998; 45: 493-501.
    • (1998) Biopolymers , vol.45 , pp. 493-501
    • Barth, A.1    Martin, S.R.2    Bayley, P.M.3
  • 62
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Struct. Funct. Bioinf. 1989; 6: 87-103.
    • (1989) Proteins: Struct. Funct. Bioinf. , vol.6 , pp. 87-103
    • Kuwajima, K.1


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