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Volumn 51, Issue 42, 2012, Pages 8338-8352

The N-methylated peptide SEN304 powerfully inhibits Aβ(1-42) toxicity by perturbing oligomer formation

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER'S DISEASE; BRAIN SLICES; DOSE-RESPONSE CURVES; ION MOBILITY-MASS SPECTROMETRY; LACTATE DEHYDROGENASE; LONG-TERM POTENTIATIONS; NEURONAL CELL; OPTIMISATIONS; PEPTIDE INHIBITORS; SDS-PAGE; SHEET FORMATION; SYNAPTOPHYSIN; THIOFLAVIN; THIOFLAVIN T; TOXICITY ASSAYS; TRAVELING WAVE;

EID: 84867757387     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300415v     Document Type: Article
Times cited : (58)

References (46)
  • 1
    • 33747484171 scopus 로고    scopus 로고
    • N-Methylated peptide inhibitors of β-amyloid aggregation and toxicity. Optimisation of inhibitor structure
    • Kokkoni, N., Stott, K., Amijee, H., Mason, J. M., and Doig, A. J. (2006) N-Methylated peptide inhibitors of β-amyloid aggregation and toxicity. Optimisation of inhibitor structure Biochemistry 45, 9906-9918
    • (2006) Biochemistry , vol.45 , pp. 9906-9918
    • Kokkoni, N.1    Stott, K.2    Amijee, H.3    Mason, J.M.4    Doig, A.J.5
  • 2
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Aβ oligomers: The solution to an Alzheimer's disease conundrum?
    • Klein, W. L., Krafft, G. A., and Finch, C. E. (2001) Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci. 24, 219-224
    • (2001) Trends Neurosci. , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 5
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • Haass, C. and Selkoe, D. J. (2007) Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide Nat. Rev. Mol. Cell Biol. 8, 101-112
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 6
    • 34248190279 scopus 로고    scopus 로고
    • Aβ Oligomers - A decade of discovery
    • Walsh, D. M. and Selkoe, D. J. (2007) Aβ Oligomers - a decade of discovery J. Neurochem. 101, 1172-1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 7
    • 33745727582 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease
    • Chauhan, V. and Chauhan, A. (2006) Oxidative stress in Alzheimer's disease Pathophysiology 13, 195-208
    • (2006) Pathophysiology , vol.13 , pp. 195-208
    • Chauhan, V.1    Chauhan, A.2
  • 9
    • 0031197194 scopus 로고    scopus 로고
    • Inhibition of amyloid formation: A strategy to delay the onset of Alzheimer's disease
    • Lansbury, P. T. J. (1997) Inhibition of amyloid formation: a strategy to delay the onset of Alzheimer's disease Curr Opin Chem Biol 1, 260-267
    • (1997) Curr Opin Chem Biol , vol.1 , pp. 260-267
    • Lansbury, P.T.J.1
  • 10
    • 34548410504 scopus 로고    scopus 로고
    • Peptide inhibitors of β-amyloid aggregation
    • Doig, A. J. (2007) Peptide inhibitors of β-amyloid aggregation Curr. Opin. Drug Discovery 10, 533-539
    • (2007) Curr. Opin. Drug Discovery , vol.10 , pp. 533-539
    • Doig, A.J.1
  • 11
    • 0034682788 scopus 로고    scopus 로고
    • Inhibition of toxicity in β-amyloid peptide fragment β(25-35) using N-methylated derivatives - A general strategy to prevent amyloid formation
    • Hughes, E., Burke, R. M., and Doig, A. J. (2000) Inhibition of toxicity in β-amyloid peptide fragment β(25-35) using N-methylated derivatives-A general strategy to prevent amyloid formation J. Biol. Chem. 275, 25109-25515
    • (2000) J. Biol. Chem. , vol.275 , pp. 25109-25515
    • Hughes, E.1    Burke, R.M.2    Doig, A.J.3
  • 12
    • 0035902507 scopus 로고    scopus 로고
    • Inhibition of β-amyloid(40) fibrillogenesis and disassembly of β-amyloid(40) fibrils by short β-amyloid cogeners containing N-methyl amino acids at alternate residues
    • Gordon, D. J., Sciaretta, K. L., and Meredith, S. C. (2001) Inhibition of β-amyloid(40) fibrillogenesis and disassembly of β-amyloid(40) fibrils by short β-amyloid cogeners containing N-methyl amino acids at alternate residues Biochemistry 40, 8237-8245
    • (2001) Biochemistry , vol.40 , pp. 8237-8245
    • Gordon, D.J.1    Sciaretta, K.L.2    Meredith, S.C.3
  • 13
    • 0036095659 scopus 로고    scopus 로고
    • Design and characterization of a membrane permeable N-methyl amino acid-containing peptide that inhibits Aβ(1-40) fibrillogenesis
    • Gordon, D. J., Tappe, R., and Meredith, S. C. (2002) Design and characterization of a membrane permeable N-methyl amino acid-containing peptide that inhibits Aβ(1-40) fibrillogenesis J. Pept. Res. 60, 37-55
    • (2002) J. Pept. Res. , vol.60 , pp. 37-55
    • Gordon, D.J.1    Tappe, R.2    Meredith, S.C.3
  • 15
    • 0036547110 scopus 로고    scopus 로고
    • Peptide inhibitors of β-amyloid aggregation
    • Findeis, M. A. (2002) Peptide inhibitors of β-amyloid aggregation Curr. Topics Med. Chem. 2, 417-423
    • (2002) Curr. Topics Med. Chem. , vol.2 , pp. 417-423
    • Findeis, M.A.1
  • 16
    • 0030746698 scopus 로고    scopus 로고
    • Design of a potent combined pseudopeptide endothelin-A/endothelin-B receptor antagonist, Ac-DBhg(16)-Leu-Asp-Ile-[NMe]Ile-Trp(21) (PD 156252): Examination of its pharmacokinetic and spectral properties
    • Cody, W. L., He, J. X., Reily, M. D., Haleen, S. J., Walker, D. M., Reyner, E. L., Stewart, B. H., and Doherty, A. M. (1997) Design of a potent combined pseudopeptide endothelin-A/endothelin-B receptor antagonist, Ac-DBhg(16)-Leu-Asp-Ile-[NMe]Ile-Trp(21) (PD 156252): Examination of its pharmacokinetic and spectral properties J. Med. Chem. 40, 2228-2240
    • (1997) J. Med. Chem. , vol.40 , pp. 2228-2240
    • Cody, W.L.1    He, J.X.2    Reily, M.D.3    Haleen, S.J.4    Walker, D.M.5    Reyner, E.L.6    Stewart, B.H.7    Doherty, A.M.8
  • 17
    • 33845309676 scopus 로고    scopus 로고
    • N-methylated cyclic pentaalanine peptides as template structures
    • Chatterjee, J., Mierke, D., and Kessler, H. (2006) N-methylated cyclic pentaalanine peptides as template structures J. Am. Chem. Soc. 128, 15164-15172
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 15164-15172
    • Chatterjee, J.1    Mierke, D.2    Kessler, H.3
  • 22
    • 0032855482 scopus 로고    scopus 로고
    • Methodological and chemical factors affecting amyloid β-peptide amyloidogenicity
    • Zagorski, M. G., Yang, J., Shao, H., Ma, K., Zeng, H., and Hong, A. (1999) Methodological and chemical factors affecting amyloid β-peptide amyloidogenicity Meth. Enzymol. 309, 189-203
    • (1999) Meth. Enzymol. , vol.309 , pp. 189-203
    • Zagorski, M.G.1    Yang, J.2    Shao, H.3    Ma, K.4    Zeng, H.5    Hong, A.6
  • 23
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of β-sheet amyloid fibril structures with Thioflavin T
    • LeVine, H. (1999) Quantification of β-sheet amyloid fibril structures with Thioflavin T Adv. Enzymol. 309, 274-284
    • (1999) Adv. Enzymol. , vol.309 , pp. 274-284
    • Levine, H.1
  • 24
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis
    • Stine, W. B., Dahlgren, K. N., Krafft, G. A., and LaDu, M. J. (2003) In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis J. Biol. Chem. 278, 11612-11622
    • (2003) J. Biol. Chem. , vol.278 , pp. 11612-11622
    • Stine, W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    Ladu, M.J.4
  • 25
    • 22844442310 scopus 로고    scopus 로고
    • Fourier transform infrared and circular dichroism spectroscopies for amyloid studies
    • Calero, M. and Gasset, M. (2005) Fourier transform infrared and circular dichroism spectroscopies for amyloid studies Methods Mol. Biol. 299, 129-151
    • (2005) Methods Mol. Biol. , vol.299 , pp. 129-151
    • Calero, M.1    Gasset, M.2
  • 26
    • 36849078628 scopus 로고    scopus 로고
    • Insight into the kinetic of amyloid β(1-42) peptide self-aggregation: Elucidation of inhibitors' mechanism of action
    • Bartolini, M., Bertucci, C., Bolognesi, M. L., Cavalli, A., Melchiorre, C., and Andrisano, V. (2007) Insight into the kinetic of amyloid β(1-42) peptide self-aggregation: elucidation of inhibitors' mechanism of action ChemBioChem 8, 2152-2161
    • (2007) ChemBioChem , vol.8 , pp. 2152-2161
    • Bartolini, M.1    Bertucci, C.2    Bolognesi, M.L.3    Cavalli, A.4    Melchiorre, C.5    Andrisano, V.6
  • 27
    • 0028118846 scopus 로고
    • Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid mediated cell death
    • Shearman, M. S., Ragan, C. I., and Iversen, L. L. (1994) Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid mediated cell death Proc. Nat. Acad. Sci. U.S.A. 91, 1470-1474
    • (1994) Proc. Nat. Acad. Sci. U.S.A. , vol.91 , pp. 1470-1474
    • Shearman, M.S.1    Ragan, C.I.2    Iversen, L.L.3
  • 28
    • 0346492847 scopus 로고    scopus 로고
    • Method for measuring neurotoxicity of aggregating polypeptides with the MTT assay on differentiated neuroblastoma cells
    • Datki, Z., Juhasz, A., Galfi, M., Soos, K., Papp, R., Zadori, D., and Penke, B. (2003) Method for measuring neurotoxicity of aggregating polypeptides with the MTT assay on differentiated neuroblastoma cells Brain Res. Bull. 62, 223-229
    • (2003) Brain Res. Bull. , vol.62 , pp. 223-229
    • Datki, Z.1    Juhasz, A.2    Galfi, M.3    Soos, K.4    Papp, R.5    Zadori, D.6    Penke, B.7
  • 29
    • 7444247272 scopus 로고    scopus 로고
    • Alzheimer's β-peptide oligomer formation at physiologic concentrations
    • LeVine, H. (2004) Alzheimer's β-peptide oligomer formation at physiologic concentrations Anal. Biochem. 335, 81-90
    • (2004) Anal. Biochem. , vol.335 , pp. 81-90
    • Levine, H.1
  • 30
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300, 486-489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 31
    • 40149094037 scopus 로고    scopus 로고
    • Ginkgolides protect against amyloid-β(1-42)-mediated synapse damage in vitro
    • Bate, C., Tayebi, M., and Williams, A. (2008) Ginkgolides protect against amyloid-β(1-42)-mediated synapse damage in vitro Mol. Neurodegen. 3, 1-9
    • (2008) Mol. Neurodegen. , vol.3 , pp. 1-9
    • Bate, C.1    Tayebi, M.2    Williams, A.3
  • 32
    • 77949895956 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids protect against prion-mediated synapse damage in vitro
    • Bate, C., Tayebi, M., Salmona, M., Diomede, L., and Williams, A. (2010) Polyunsaturated fatty acids protect against prion-mediated synapse damage in vitro Neurotox. Res. 17, 203-214
    • (2010) Neurotox. Res. , vol.17 , pp. 203-214
    • Bate, C.1    Tayebi, M.2    Salmona, M.3    Diomede, L.4    Williams, A.5
  • 33
    • 78649740289 scopus 로고    scopus 로고
    • α-synuclein induced synapse damage is enhanced by Aβ1-42
    • Bate, C., Gentleman, S., and Williams, A. (2010) α-synuclein induced synapse damage is enhanced by Aβ1-42 Mol. Neurodegener. 5, 55
    • (2010) Mol. Neurodegener. , vol.5 , pp. 55
    • Bate, C.1    Gentleman, S.2    Williams, A.3
  • 34
    • 22144462135 scopus 로고    scopus 로고
    • Neurotoxic protein oligomers - What you see is not always what you get
    • Bitan, G., Fradinger, E. A., Spring, S. M., and Teplow, D. B. (2005) Neurotoxic protein oligomers-what you see is not always what you get Amyloid 12, 88-95
    • (2005) Amyloid , vol.12 , pp. 88-95
    • Bitan, G.1    Fradinger, E.A.2    Spring, S.M.3    Teplow, D.B.4
  • 35
    • 34249860495 scopus 로고    scopus 로고
    • Small-molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct
    • Necula, M., Kayed, R., Milton, S., and Glabe, C. G. (2007) Small-molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct J. Biol. Chem. 282, 10311-10324
    • (2007) J. Biol. Chem. , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 36
    • 0034647786 scopus 로고    scopus 로고
    • Oligomerization and toxicity of β-amyloid-42 implicated in Alzheimer's disease
    • El-Agnaf, O. M., Mahil, D. S., Patel, B. P., and Austen, B. M. (2000) Oligomerization and toxicity of β-amyloid-42 implicated in Alzheimer's disease Biochem. Biophys. Res. Commun. 273, 1003-1007
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 1003-1007
    • El-Agnaf, O.M.1    Mahil, D.S.2    Patel, B.P.3    Austen, B.M.4
  • 38
    • 0027758904 scopus 로고
    • Synaptic vesicle proteins and regulated exocytosis
    • Elferink, L. A. and Scheller, R. H. (1993) Synaptic vesicle proteins and regulated exocytosis J. Cell. Sci. Suppl. 17, 75-79
    • (1993) J. Cell. Sci. Suppl. , vol.17 , pp. 75-79
    • Elferink, L.A.1    Scheller, R.H.2
  • 39
    • 0024595972 scopus 로고
    • Synaptic loss in Alzheimer's disease and other dementias
    • Hamos, J. E., DeGennaro, L. J., and Drachman, D. A. (1989) Synaptic loss in Alzheimer's disease and other dementias Neurology 39, 355-361
    • (1989) Neurology , vol.39 , pp. 355-361
    • Hamos, J.E.1    Degennaro, L.J.2    Drachman, D.A.3
  • 40
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
    • DeKosky, S. T. and Scheff, S. W. (1990) Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity Ann. Neurol. 27, 457-464
    • (1990) Ann. Neurol. , vol.27 , pp. 457-464
    • Dekosky, S.T.1    Scheff, S.W.2
  • 41
    • 34547550818 scopus 로고    scopus 로고
    • Squalestatin protects neurons and reduces the activation of cytoplasmic phospholipase A2 by Aβ(1-42)
    • Bate, C. and Williams, A. (2007) Squalestatin protects neurons and reduces the activation of cytoplasmic phospholipase A2 by Aβ(1-42) Neuropharmacology 53, 222-231
    • (2007) Neuropharmacology , vol.53 , pp. 222-231
    • Bate, C.1    Williams, A.2
  • 44
    • 0035866076 scopus 로고    scopus 로고
    • Use-dependent effects of amyloidogenic fragments of beta-amyloid precursor protein on synaptic plasticity in rat hippocampus in vivo
    • Kim, J. H., Anwyl, R., Suh, Y. H., Djamgoz, M. B. A., and Rowan, M. J. (2001) Use-dependent effects of amyloidogenic fragments of beta-amyloid precursor protein on synaptic plasticity in rat hippocampus in vivo J. Neurosci. 21, 1327-1333
    • (2001) J. Neurosci. , vol.21 , pp. 1327-1333
    • Kim, J.H.1    Anwyl, R.2    Suh, Y.H.3    Djamgoz, M.B.A.4    Rowan, M.J.5
  • 45
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., and Selkoe, D. J. (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo Nature 416, 535-539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8


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