메뉴 건너뛰기




Volumn 19, Issue 9, 2005, Pages 1051-1055

A model for the role of short self-assembled peptides in the very early stages of the origin of life

Author keywords

stacking; Aromatic interactions; Closed cage nanostructures; Molecular recognition; Origin of life; Peptides; Self association

Indexed keywords

AMYLOID; DIPEPTIDE; NUCLEIC ACID; OLIGONUCLEOTIDE; RNA; TRIPEPTIDE;

EID: 21744439797     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.04-3256hyp     Document Type: Review
Times cited : (106)

References (51)
  • 2
    • 0033817722 scopus 로고    scopus 로고
    • Accretion of moon and earth and the emergence of life
    • Arrhenius, G., and Lepland, A. (2000) Accretion of moon and earth and the emergence of life. Chem. Geol. 169, 69-82
    • (2000) Chem. Geol. , vol.169 , pp. 69-82
    • Arrhenius, G.1    Lepland, A.2
  • 3
    • 0032493439 scopus 로고    scopus 로고
    • The stability of the RNA bases: Implications for the origin of life
    • Levy, M., and Miller, S. L. (1998) The stability of the RNA bases: implications for the origin of life. Proc. Natl. Acad. Sci. USA 95, 7933-7938
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7933-7938
    • Levy, M.1    Miller, S.L.2
  • 4
    • 0023823426 scopus 로고
    • Impact frustration of the origin of life
    • Maher, K. A., and Stevenson, D. J. (1988) Impact frustration of the origin of life. Nature (London) 331, 612-614
    • (1988) Nature (London) , vol.331 , pp. 612-614
    • Maher, K.A.1    Stevenson, D.J.2
  • 5
    • 3042709433 scopus 로고    scopus 로고
    • Prebiotic chemistry and the origin of the RNA world
    • Orgel, L. E. (2004) Prebiotic chemistry and the origin of the RNA world. Crit. Rev. Biochem. Mol. Biol. 39, 99-123
    • (2004) Crit. Rev. Biochem. Mol. Biol. , vol.39 , pp. 99-123
    • Orgel, L.E.1
  • 6
    • 0032768196 scopus 로고    scopus 로고
    • Peptides and the origin of life
    • Rode, B. M. (1998) Peptides and the origin of life. Peptides 20, 773-786
    • (1998) Peptides , vol.20 , pp. 773-786
    • Rode, B.M.1
  • 7
    • 0001680356 scopus 로고
    • Photosynthesis of amino acids from paraformaldehyde involving the fixation of nitrogen in the presence of colloidal molybdenum oxide as catalyst
    • Bahadur, K., Ranganayaki, S., and Santamaria, L. (1958) Photosynthesis of amino acids from paraformaldehyde involving the fixation of nitrogen in the presence of colloidal molybdenum oxide as catalyst. Nature (London) 182, 1668
    • (1958) Nature (London) , vol.182 , pp. 1668
    • Bahadur, K.1    Ranganayaki, S.2    Santamaria, L.3
  • 8
    • 3242815603 scopus 로고    scopus 로고
    • Prebiotic formation of amino acids in a neutral atmosphere by electric discharge
    • Plankensteiner, K., Reiner, H., Schranz, B., and Rode, B. M. (2004) Prebiotic formation of amino acids in a neutral atmosphere by electric discharge. Angew. Chem. Int. Ed. Engl. 43, 1886-1888
    • (2004) Angew. Chem. Int. Ed. Engl. , vol.43 , pp. 1886-1888
    • Plankensteiner, K.1    Reiner, H.2    Schranz, B.3    Rode, B.M.4
  • 9
    • 0024972533 scopus 로고
    • Pre-biotic organic matter from comets and asteroids
    • Anders, E. (1989) Pre-biotic organic matter from comets and asteroids. Nature (London) 342, 255-257
    • (1989) Nature (London) , vol.342 , pp. 255-257
    • Anders, E.1
  • 10
    • 0033303314 scopus 로고    scopus 로고
    • The possible role of Cu (II) for the origin of life
    • Rode, B. M., and Suwannachot, Y. (1999) The possible role of Cu (II) for the origin of life. Coord. Chem. Rev. 192, 1085-1099
    • (1999) Coord. Chem. Rev. , vol.192 , pp. 1085-1099
    • Rode, B.M.1    Suwannachot, Y.2
  • 11
    • 3142758746 scopus 로고    scopus 로고
    • A small aptamer with strong and specific recognition of the triphosphate of ATP
    • Sazani, P. L., Larralde, R., and Szostak, J. W. (2004) A small aptamer with strong and specific recognition of the triphosphate of ATP. J. Am. Chem. Soc. 126, 8370-8371
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8370-8371
    • Sazani, P.L.1    Larralde, R.2    Szostak, J.W.3
  • 12
    • 0642306490 scopus 로고    scopus 로고
    • The origins of RNA catalysis in ribozymes. Trends Biochem
    • Lilley, D. M. (2003) The origins of RNA catalysis in ribozymes. Trends Biochem. Sci. 28, 495-501
    • (2003) Sci. , vol.28 , pp. 495-501
    • Lilley, D.M.1
  • 13
    • 0037381618 scopus 로고    scopus 로고
    • RNA sensors and riboswitches: Self-regulating messages
    • Lai, E. C. (2003) RNA sensors and riboswitches: self-regulating messages. Curr. Biol. 13, R285-R291
    • (2003) Curr. Biol. , vol.13
    • Lai, E.C.1
  • 14
    • 0029111395 scopus 로고
    • Rates of decomposition of ribose and other sugars: Implications for chemical evolution
    • Larralde, R., Robertson, M. P., and Miller, S. L. (1995) Rates of decomposition of ribose and other sugars: implications for chemical evolution. Proc. Natl. Acad. Sci. USA 92, 8158-8160
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8158-8160
    • Larralde, R.1    Robertson, M.P.2    Miller, S.L.3
  • 15
    • 0029160308 scopus 로고    scopus 로고
    • Template switching between PNA and RNA oligonucleotides
    • Böhler, C., Nielsen, P. E., and Orgel, L. E. (2002) Template switching between PNA and RNA oligonucleotides. Nature (London) 376, 578-581
    • (2002) Nature (London) , vol.376 , pp. 578-581
    • Böhler, C.1    Nielsen, P.E.2    Orgel, L.E.3
  • 18
    • 0023785307 scopus 로고
    • The evolutionary transition from RNA to DNA in early cells
    • Lazcano, A., Gariglio, P., Margulis, L., and Oro, J. (1988) The evolutionary transition from RNA to DNA in early cells. J. Mol. Evol. 27, 283-290
    • (1988) J. Mol. Evol. , vol.27 , pp. 283-290
    • Lazcano, A.1    Gariglio, P.2    Margulis, L.3    Oro, J.4
  • 19
    • 0001608018 scopus 로고    scopus 로고
    • Self-assembly of surfactant-like peptides with variable glycine tails to form nanotubes and nanovesicles
    • Santoso, S., Hwang, W., Hartman, H., and Zhang, S. (2002) Self-assembly of surfactant-like peptides with variable glycine tails to form nanotubes and nanovesicles. Nano Lett. 2, 687-691
    • (2002) Nano Lett. , vol.2 , pp. 687-691
    • Santoso, S.1    Hwang, W.2    Hartman, H.3    Zhang, S.4
  • 21
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. (2003) Protein folding and misfolding. Nature (London) 426, 884-890
    • (2003) Nature (London) , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 22
    • 0035187228 scopus 로고    scopus 로고
    • Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain
    • Chiti, F., Bucciantini, M., Capanni, C., Taddei, N., Dobson, C. M., and Stefani, M. (2001) Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain. Protein Sci. 10, 2541-2547
    • (2001) Protein Sci. , vol.10 , pp. 2541-2547
    • Chiti, F.1    Bucciantini, M.2    Capanni, C.3    Taddei, N.4    Dobson, C.M.5    Stefani, M.6
  • 23
    • 0037126833 scopus 로고    scopus 로고
    • The "Correctly Folded" state of proteins: Is it a metastable state?
    • Gazit, E. (2002) The "Correctly Folded" state of proteins: is it a metastable state? Angew. Chem. Int. Ed. Engl. 41, 257-259
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 257-259
    • Gazit, E.1
  • 24
    • 0035823724 scopus 로고    scopus 로고
    • First crystallographic signature of amyloid-like fibril forming beta-sheet assemblage from a tripeptide with non-coded amino acids
    • Maji, S. K., Drew, M. G., and Banerjee, A. (2001) First crystallographic signature of amyloid-like fibril forming beta-sheet assemblage from a tripeptide with non-coded amino acids. Chem. Commun. (Cambridge) 1946-1947
    • (2001) Chem. Commun. (Cambridge) , pp. 1946-1947
    • Maji, S.K.1    Drew, M.G.2    Banerjee, A.3
  • 25
    • 0037144424 scopus 로고    scopus 로고
    • Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin
    • Reches, M., Porat, Y., and Gazit, E. (2002) Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin. J. Biol. Chem. 277, 35475-35480
    • (2002) J. Biol. Chem. , vol.277 , pp. 35475-35480
    • Reches, M.1    Porat, Y.2    Gazit, E.3
  • 27
    • 0037044732 scopus 로고    scopus 로고
    • Charge attraction and beta propensity are necessary for amyloid fibril formation from tetrapeptides
    • Tjernberg, L., Hosia, W., Bark, N., Thyberg, J., and Johansson, J. (2002) Charge attraction and beta propensity are necessary for amyloid fibril formation from tetrapeptides. J. Biol. Chem. 277, 43243-43246
    • (2002) J. Biol. Chem. , vol.277 , pp. 43243-43246
    • Tjernberg, L.1    Hosia, W.2    Bark, N.3    Thyberg, J.4    Johansson, J.5
  • 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., and Zhang, S. (2002) Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles. Proc. Natl. Acad. Sci. USA 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
  • 29
    • 0037466613 scopus 로고    scopus 로고
    • Casting metal nanowires within discrete self-assembled peptide nanotubes
    • Reches, M., and Gazit, E. (2003) Casting metal nanowires within discrete self-assembled peptide nanotubes. Science 300, 625-627
    • (2003) Science , vol.300 , pp. 625-627
    • Reches, M.1    Gazit, E.2
  • 31
    • 2342595738 scopus 로고    scopus 로고
    • Formation of closed-cage nanostructures by self-assembly of aromatic dipeptides
    • Reches, M., and Gazit, E. (2004) Formation of closed-cage nanostructures by self-assembly of aromatic dipeptides. Nano Lett. 4, 581-585
    • (2004) Nano Lett. , vol.4 , pp. 581-585
    • Reches, M.1    Gazit, E.2
  • 32
    • 0033383044 scopus 로고    scopus 로고
    • Are prions a relic of an early stage of peptide evolution?
    • Rode, B. M., Flader, W., Sotriffer, C., and Righi, A. (1999) Are prions a relic of an early stage of peptide evolution? Peptides 20, 1513-1516
    • (1999) Peptides , vol.20 , pp. 1513-1516
    • Rode, B.M.1    Flader, W.2    Sotriffer, C.3    Righi, A.4
  • 33
    • 0842323862 scopus 로고    scopus 로고
    • Chemical evolution and meteorites: An update
    • Pizzarello, S. (2004) Chemical evolution and meteorites: an update. Orig. Life Evol. Biosph. 34, 25-34
    • (2004) Orig. Life Evol. Biosph. , vol.34 , pp. 25-34
    • Pizzarello, S.1
  • 35
    • 0842305210 scopus 로고    scopus 로고
    • Construction of a chemically and conformationally self-replicating system of amyloid-like fibrils
    • Takahashi, Y., and Mihara, H. (2004) Construction of a chemically and conformationally self-replicating system of amyloid-like fibrils. Bioorg. Med. Chem. 12, 693-699
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 693-699
    • Takahashi, Y.1    Mihara, H.2
  • 36
    • 0036135139 scopus 로고    scopus 로고
    • A possible role for π-stacking in the self-assembly of amyloid fibrils
    • Gazit, E. (2002) A possible role for π-stacking in the self-assembly of amyloid fibrils. FASEB J. 16, 77-83
    • (2002) FASEB J. , vol.16 , pp. 77-83
    • Gazit, E.1
  • 37
    • 3042584515 scopus 로고    scopus 로고
    • The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates
    • Tartaglia, G. G., Cavalli, A., Pellarin, R., and Caflisch, A. (2004) The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates. Protein Sci. 13, 1939-1941
    • (2004) Protein Sci. , vol.13 , pp. 1939-1941
    • Tartaglia, G.G.1    Cavalli, A.2    Pellarin, R.3    Caflisch, A.4
  • 38
    • 0842307662 scopus 로고    scopus 로고
    • Structural diversity of amyloid fibril formed in human calcitonin as revealed by site-directed C-13 solid-state NMR spectroscopy
    • Naito, A., Kamihira, M., Inoue, R., and Saito, H. (2004) Structural diversity of amyloid fibril formed in human calcitonin as revealed by site-directed C-13 solid-state NMR spectroscopy. Magn. Reson. Chem. 42, 247-257
    • (2004) Magn. Reson. Chem. , vol.42 , pp. 247-257
    • Naito, A.1    Kamihira, M.2    Inoue, R.3    Saito, H.4
  • 39
    • 0034837523 scopus 로고    scopus 로고
    • Molecular dynamics and thermodynamics of protein-RNA interactions: Mutation of a conserved aromatic residue modifies stacking interactions and structural adaptation in the U1A-stem loop 2 RNA complex
    • Blakaj, D. M., McConnell, K. J., Beveridge, D. L., and Baranger, A. M. (2001) Molecular dynamics and thermodynamics of protein-RNA interactions: mutation of a conserved aromatic residue modifies stacking interactions and structural adaptation in the U1A-stem loop 2 RNA complex. J. Am. Chem. Soc. 123, 2548-2551
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2548-2551
    • Blakaj, D.M.1    McConnell, K.J.2    Beveridge, D.L.3    Baranger, A.M.4
  • 40
    • 0034716346 scopus 로고    scopus 로고
    • Coupling rational design with libraries leads to the production of an ATP selective chemosensor
    • Schneider, S., O'Neil, S., and Anslyn, E. V. (2000) coupling rational design with libraries leads to the production of an ATP selective chemosensor. J. Am. Chem. Soc. 122, 542-543
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 542-543
    • Schneider, S.1    O'Neil, S.2    Anslyn, E.V.3
  • 42
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett, J. T., and Lansbury, P. T., Jr. (1993) Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 43
    • 1042302877 scopus 로고    scopus 로고
    • A peptide flavoprotein mimic: Flavin recognition and redox potential modulation in water by a designed beta hairpin
    • Butterfield, S. M., Goodman, C. M., Rotello, V. M., and Waters, M. L. (2004) A peptide flavoprotein mimic: flavin recognition and redox potential modulation in water by a designed beta hairpin. Angew. Chem. Int. Ed. Engl. 43, 724-727
    • (2004) Angew. Chem. Int. Ed. Engl. , vol.43 , pp. 724-727
    • Butterfield, S.M.1    Goodman, C.M.2    Rotello, V.M.3    Waters, M.L.4
  • 44
    • 0041624420 scopus 로고    scopus 로고
    • A designed beta-hairpin peptide for molecular recognition of ATP in water
    • Butterfield, S. M., and Waters, M. L. (2003) A designed beta-hairpin peptide for molecular recognition of ATP in water. J. Am. Chem. Soc. 125, 9580-9581
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9580-9581
    • Butterfield, S.M.1    Waters, M.L.2
  • 45
    • 0030819170 scopus 로고    scopus 로고
    • Substrate-directed formation of small biocatalysts under prebiotic conditions
    • Kochavi, E., Bar-Nun, A., and Fleminger, G. (1997) Substrate-directed formation of small biocatalysts under prebiotic conditions. J. Mol. Evol. 45, 342-351
    • (1997) J. Mol. Evol. , vol.45 , pp. 342-351
    • Kochavi, E.1    Bar-Nun, A.2    Fleminger, G.3
  • 47
    • 0029583784 scopus 로고
    • Stacking free energy profiles for all 16 natural ribodinucleoside monophosphates in aqueous solution?
    • Norberg, J., and Nilsson, L. (1995) Stacking free energy profiles for all 16 natural ribodinucleoside monophosphates in aqueous solution? J. Am. Chem. Soc. 117, 10832-10840
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10832-10840
    • Norberg, J.1    Nilsson, L.2
  • 48
    • 0037079679 scopus 로고    scopus 로고
    • Investigation of a conserved stacking interaction in target site recognition by the U1A protein
    • Shiels, J. C., Tuite, J. B., Nolan, S. J., and Baranger, A. M. (2002) Investigation of a conserved stacking interaction in target site recognition by the U1A protein. Nucleic Acids Res. 30, 550-558
    • (2002) Nucleic Acids Res. , vol.30 , pp. 550-558
    • Shiels, J.C.1    Tuite, J.B.2    Nolan, S.J.3    Baranger, A.M.4
  • 49
    • 0031860374 scopus 로고    scopus 로고
    • RNA recognition by RNP proteins during RNA processing
    • Gabriele, V., and Kiyoshi, N. (1998) RNA recognition by RNP proteins during RNA processing. Annu. Rev. Biophys. Biomol. Struct. 27, 407-445
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 407-445
    • Gabriele, V.1    Kiyoshi, N.2
  • 50
    • 0036015843 scopus 로고    scopus 로고
    • A selected ribozyme catalyzing diverse dipeptide synthesis
    • Sun, L., Cui, Z., Gottlieb, R. L., and Zhang, B. (2002) A selected ribozyme catalyzing diverse dipeptide synthesis. Chem. Biol. 9, 619-628
    • (2002) Chem. Biol. , vol.9 , pp. 619-628
    • Sun, L.1    Cui, Z.2    Gottlieb, R.L.3    Zhang, B.4
  • 51
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.