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Volumn 274, Issue 24, 2007, Pages 6415-6425

Inhibition of amyloid fibrillation of lysozyme by indole derivatives - Possible mechanism of action

Author keywords

Amyloid inhibition; Docking; Indole derivative; Lysozyme; Organic solvent

Indexed keywords

3 INDOLEMETHANOL; AMYLOID; CONGO RED; EGG WHITE; INDOLE ALDEHYDE; INDOLE DERIVATIVE; INDOLEACETIC ACID; LYSOZYME; THIOFLAVINE; TRYPTOPHAN; TRYPTOPHOL; UNCLASSIFIED DRUG;

EID: 36749011905     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06158.x     Document Type: Article
Times cited : (135)

References (47)
  • 1
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor JP, Hardy J Fischbeck KH (2002) Toxic proteins in neurodegenerative disease. Science 296, 1991 1995.
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 2
    • 0035961291 scopus 로고    scopus 로고
    • Pathogenesis, diagnosis and treatment of systemic amyloidosis
    • Pepys MB (2001) Pathogenesis, diagnosis and treatment of systemic amyloidosis. Phil Trans R Soc Lond B Biol Sci 356, 203 210.
    • (2001) Phil Trans R Soc Lond B Biol Sci , vol.356 , pp. 203-210
    • Pepys, M.B.1
  • 3
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75, 333 366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 4
    • 33845652277 scopus 로고    scopus 로고
    • Structural models of amyloid-like fibrils
    • Nelson R Eisenberg D (2006) Structural models of amyloid-like fibrils. Adv Protein Chem 73, 235 282.
    • (2006) Adv Protein Chem , vol.73 , pp. 235-282
    • Nelson, R.1    Eisenberg, D.2
  • 6
    • 0036669903 scopus 로고    scopus 로고
    • Examining the structure of the mature amyloid fibril
    • Makin OS Serpell LC (2002) Examining the structure of the mature amyloid fibril. Biochem Soc Trans 30, 521 525.
    • (2002) Biochem Soc Trans , vol.30 , pp. 521-525
    • Makin, O.S.1    Serpell, L.C.2
  • 7
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde M Blake C (1997) The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv Protein Chem 50, 123 159.
    • (1997) Adv Protein Chem , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 9
    • 28244437028 scopus 로고    scopus 로고
    • The Yin and Yang of protein folding
    • Jahn TR Radford SE (2005) The Yin and Yang of protein folding. FEBS J 272, 5962 5970.
    • (2005) FEBS J , vol.272 , pp. 5962-5970
    • Jahn, T.R.1    Radford, S.E.2
  • 10
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM (2003) Protein folding and misfolding. Nature 426, 884 890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 13
    • 33645929400 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation and cytotoxicity by hydroxyindole derivatives
    • Cohen T, Frydman-Marom A, Rechter M Gazit E (2006) Inhibition of amyloid fibril formation and cytotoxicity by hydroxyindole derivatives. Biochemistry 45, 4727 4735.
    • (2006) Biochemistry , vol.45 , pp. 4727-4735
    • Cohen, T.1    Frydman-Marom, A.2    Rechter, M.3    Gazit, E.4
  • 15
    • 33644919388 scopus 로고    scopus 로고
    • Doxycycline disrupts transthyretin amyloid: Evidence from studies in a FAP transgenic mice model
    • Cardoso I Saraiva MJ (2006) Doxycycline disrupts transthyretin amyloid: evidence from studies in a FAP transgenic mice model. FASEB J 20, 234 239.
    • (2006) FASEB J , vol.20 , pp. 234-239
    • Cardoso, I.1    Saraiva, M.J.2
  • 16
    • 1542327644 scopus 로고    scopus 로고
    • Ligand-dependent inhibition and reversal of tau filament formation
    • Chirita C, Necula M Kuret J (2004) Ligand-dependent inhibition and reversal of tau filament formation. Biochemistry 43, 2879 2887.
    • (2004) Biochemistry , vol.43 , pp. 2879-2887
    • Chirita, C.1    Necula, M.2    Kuret, J.3
  • 17
    • 8844224948 scopus 로고    scopus 로고
    • Rifampicin inhibits alpha-synuclein fibrillation and disaggregates fibrils
    • Li J, Zhu M, Rajamani S, Uversky VN Fink AL (2004) Rifampicin inhibits alpha-synuclein fibrillation and disaggregates fibrils. Chem Biol 11, 1513 1521.
    • (2004) Chem Biol , vol.11 , pp. 1513-1521
    • Li, J.1    Zhu, M.2    Rajamani, S.3    Uversky, V.N.4    Fink, A.L.5
  • 18
    • 33644945380 scopus 로고    scopus 로고
    • Antioxidant compounds have potent anti-fibrillogenic and fibril-destabilizing effects for alpha-synuclein fibrils in vitro
    • Ono K Yamada M (2006) Antioxidant compounds have potent anti-fibrillogenic and fibril-destabilizing effects for alpha-synuclein fibrils in vitro. J Neurochem 97, 105 115.
    • (2006) J Neurochem , vol.97 , pp. 105-115
    • Ono, K.1    Yamada, M.2
  • 19
    • 0035085736 scopus 로고    scopus 로고
    • Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation
    • Chiti F, Taddei N, Stefani M, Dobson CM Ramponi G (2001) Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation. Protein Sci 10, 879 886.
    • (2001) Protein Sci , vol.10 , pp. 879-886
    • Chiti, F.1    Taddei, N.2    Stefani, M.3    Dobson, C.M.4    Ramponi, G.5
  • 20
    • 33749243722 scopus 로고    scopus 로고
    • Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway
    • Soldi G, Plakoutsi G, Taddei N Chiti F (2006) Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway. J Med Chem 49, 6057 6064.
    • (2006) J Med Chem , vol.49 , pp. 6057-6064
    • Soldi, G.1    Plakoutsi, G.2    Taddei, N.3    Chiti, F.4
  • 21
    • 21744452155 scopus 로고    scopus 로고
    • Kinetic stabilization of an oligomeric protein under physiological conditions demonstrated by a lack of subunit exchange: Implications for transthyretin amyloidosis
    • Wiseman RL, Green NS Kelly JW (2005) Kinetic stabilization of an oligomeric protein under physiological conditions demonstrated by a lack of subunit exchange: implications for transthyretin amyloidosis. Biochemistry 44, 9265 9274.
    • (2005) Biochemistry , vol.44 , pp. 9265-9274
    • Wiseman, R.L.1    Green, N.S.2    Kelly, J.W.3
  • 22
    • 0033618295 scopus 로고    scopus 로고
    • Potent neuroprotective properties against the Alzheimer β-amyloid by an endogenous melatonin-related indole structure, indole-3-propionic acid
    • Chyan YJ, Poeggeler B, Omar RA, Chain DG, Frangione B, Ghiso J Pappolla MA (1999) Potent neuroprotective properties against the Alzheimer β-amyloid by an endogenous melatonin-related indole structure, indole-3-propionic acid. J Biol Chem 274, 21937 21942.
    • (1999) J Biol Chem , vol.274 , pp. 21937-21942
    • Chyan, Y.J.1    Poeggeler, B.2    Omar, R.A.3    Chain, D.G.4    Frangione, B.5    Ghiso, J.6    Pappolla, M.A.7
  • 24
    • 34047133423 scopus 로고    scopus 로고
    • Indole derivatives as potent inhibitors of 5-lipoxygenase: Design, synthesis, biological evaluation, and molecular modeling
    • Zheng M, Zheng M, Ye D, Deng Y, Qiu S, Luo X, Chen K, Liu H Jiang H (2007) Indole derivatives as potent inhibitors of 5-lipoxygenase: design, synthesis, biological evaluation, and molecular modeling. Bioorg Med Chem Lett 17, 2414 2420.
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 2414-2420
    • Zheng, M.1    Zheng, M.2    Ye, D.3    Deng, Y.4    Qiu, S.5    Luo, X.6    Chen, K.7    Liu, H.8    Jiang, H.9
  • 25
    • 33751099101 scopus 로고    scopus 로고
    • Indole-3-carbinol mediated cell cycle arrest of LNCaP human prostate cancer cells requires the induced production of activated p53 tumor suppressor protein
    • Hsu JC, Dev A, Wing A, Brew CT, Bjeldanes LF Firestone GL (2006) Indole-3-carbinol mediated cell cycle arrest of LNCaP human prostate cancer cells requires the induced production of activated p53 tumor suppressor protein. Biochem Pharmacol 72, 1714 1723.
    • (2006) Biochem Pharmacol , vol.72 , pp. 1714-1723
    • Hsu, J.C.1    Dev, A.2    Wing, A.3    Brew, C.T.4    Bjeldanes, L.F.5    Firestone, G.L.6
  • 27
    • 33645988190 scopus 로고    scopus 로고
    • Organofluorine inhibitors of amyloid fibrillogenesis
    • Torok M, Abid M, Mhadgut SC Torok B (2006) Organofluorine inhibitors of amyloid fibrillogenesis. Biochemistry 45, 5377 5383.
    • (2006) Biochemistry , vol.45 , pp. 5377-5383
    • Torok, M.1    Abid, M.2    Mhadgut, S.C.3    Torok, B.4
  • 29
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of 'aggregation-prone' and 'aggregation-susceptible' regions in proteins associated with neurodegenerative diseases
    • Pawar AP, Dubay KF, Zurdo J, Chiti F, Vendruscolo M Dobson CM (2005) Prediction of 'aggregation-prone' and 'aggregation-susceptible' regions in proteins associated with neurodegenerative diseases. J Mol Biol 350, 379 392.
    • (2005) J Mol Biol , vol.350 , pp. 379-392
    • Pawar, A.P.1    Dubay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 30
    • 0036135139 scopus 로고    scopus 로고
    • The possible role for pi-stacking in the self-assembly of amyloid fibrils
    • Gazit E (2002) The possible role for pi-stacking in the self-assembly of amyloid fibrils. FASEB 16, 77 83.
    • (2002) FASEB , vol.16 , pp. 77-83
    • Gazit, E.1
  • 31
    • 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 (2006) Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase. Protein Sci 15, 862 870.
    • (2006) Protein Sci , vol.15 , pp. 862-870
    • Bemporad, F.1    Taddei, N.2    Stefani, M.3    Chiti, F.4
  • 32
    • 22144448838 scopus 로고    scopus 로고
    • The role of Phe in the formation of well-ordered oligomers of amyloidogenic hexapeptide (NFGAIL) observed in molecular dynamics simulations with explicit solvent
    • Wu C, Lei H Duan Y (2005) The role of Phe in the formation of well-ordered oligomers of amyloidogenic hexapeptide (NFGAIL) observed in molecular dynamics simulations with explicit solvent. Biophys J 88, 2897 2906.
    • (2005) Biophys J , vol.88 , pp. 2897-2906
    • Wu, C.1    Lei, H.2    Duan, Y.3
  • 33
    • 0035349804 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's disease β-amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols: Implications for Alzheimer's therapy
    • De Felice FG, Houzel J, Garcia-Abreu J, Louzada PR, Afonso RC, Meirelles ML, Lent R, Neto VM Ferreira ST (2001) Inhibition of Alzheimer's disease β-amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols: implications for Alzheimer's therapy. FASEB J 15, 1297 1299.
    • (2001) FASEB J , vol.15 , pp. 1297-1299
    • De Felice, F.G.1    Houzel, J.2    Garcia-Abreu, J.3    Louzada, P.R.4    Afonso, R.C.5    Meirelles, M.L.6    Lent, R.7    Neto, V.M.8    Ferreira, S.T.9
  • 34
    • 10844254749 scopus 로고    scopus 로고
    • Role of aromatic interactions in amyloid formation by peptides derived from human amylin
    • Tracz SM, Abedini A, Driscoll M Raleigh DP (2004) Role of aromatic interactions in amyloid formation by peptides derived from human amylin. Biochemistry 43, 15901 15908.
    • (2004) Biochemistry , vol.43 , pp. 15901-15908
    • Tracz, S.M.1    Abedini, A.2    Driscoll, M.3    Raleigh, D.P.4
  • 35
    • 11244340520 scopus 로고    scopus 로고
    • Thermally induced fibrillar aggregation of hen egg white lysozyme
    • Arnaudov LN de Vries R (2005) Thermally induced fibrillar aggregation of hen egg white lysozyme. Biophys J 88, 515 526.
    • (2005) Biophys J , vol.88 , pp. 515-526
    • Arnaudov, L.N.1    De Vries, R.2
  • 39
    • 0015505519 scopus 로고
    • The inhibition of HEWL by imidazole and indole derivatives
    • Swan ID (1972) The inhibition of HEWL by imidazole and indole derivatives. J Mol Biol 65, 59 62.
    • (1972) J Mol Biol , vol.65 , pp. 59-62
    • Swan, I.D.1
  • 41
    • 33344463679 scopus 로고    scopus 로고
    • Common mechanisms of amyloid oligomer pathogenesis in degenerative disease
    • Glabe CG (2006) Common mechanisms of amyloid oligomer pathogenesis in degenerative disease. Neurobiol Aging 27, 570 575.
    • (2006) Neurobiol Aging , vol.27 , pp. 570-575
    • Glabe, C.G.1
  • 42
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • Fink AL Uversky VN (2004) Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim Biophys Acta 1698, 131 153.
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 131-153
    • Fink, A.L.1    Uversky, V.N.2
  • 43
    • 0025778735 scopus 로고
    • Lysozyme revisited: Crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D
    • Strynadka NC James MN (1991) Lysozyme revisited: crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D. J Mol Biol 220, 401 424.
    • (1991) J Mol Biol , vol.220 , pp. 401-424
    • Strynadka, N.C.1    James, M.N.2
  • 44
    • 0026514355 scopus 로고
    • Spectrofluorimetric assessment of the surface hydrophobicity of proteins
    • Cardamone M Puri NK (1992) Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochem J 282, 589 593.
    • (1992) Biochem J , vol.282 , pp. 589-593
    • Cardamone, M.1    Puri, N.K.2
  • 45
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson MR (2004) Techniques to study amyloid fibril formation in vitro. Methods 34, 151 160.
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 46
    • 0024352110 scopus 로고
    • Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • Klunk WE, Pettegrew JW Abraham DJ (1989) Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J Histochem Cytochem 37, 1273 1281.
    • (1989) J Histochem Cytochem , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 47
    • 0023476453 scopus 로고
    • Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces
    • Sackett DL Wolff J (1987) Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces. Anal Biochem 167, 228 234.
    • (1987) Anal Biochem , vol.167 , pp. 228-234
    • Sackett, D.L.1    Wolff, J.2


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