메뉴 건너뛰기




Volumn 84, Issue , 2012, Pages 49-52

Modulation of fibril formation by a beta-sheet breaker peptide ligand: An electrochemical approach

Author keywords

Alzheimer's disease; Amyloid ; Fluorescence; Square wave voltammetry; Thioflavin T

Indexed keywords

ALZHEIMER'S DISEASE; AMYLOID FIBRIL; BETA-SHEET; CARBON STRIPS; ELECTROCHEMICAL ANALYSIS; ELECTROCHEMICAL SIGNALS; FIBRIL FORMATION; FLUORESCENCE ANALYSIS; FLUORESCENT MARKERS; IN-VITRO; LABEL FREE; MEDICAL NEEDS; PEPTIDE LIGAND; SCREEN-PRINTED; SHEET FORMATION; SQUARE WAVE VOLTAMMETRY; THIOFLAVIN T; TIME-SCALES;

EID: 84155163206     PISSN: 15675394     EISSN: 1878562X     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2011.08.007     Document Type: Article
Times cited : (37)

References (23)
  • 3
    • 0037135111 scopus 로고    scopus 로고
    • Medicine-the amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., Selkoe D.J. Medicine-the amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 4
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75:333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 5
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C., Davis J.B., Lesley R., Schubert D. Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 1994, 77:817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 6
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state
    • Pike C.J., Burdick D., Walencewicz A.J., Glabe C.G., Gotman C.W. Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 1993, 13:1676-1687.
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Gotman, C.W.5
  • 8
    • 0026619343 scopus 로고
    • Substitutions of hydrophobic amino-acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides
    • Hilbich C., Kisterswoike B., Reed J., Masters C.L., Beyreuther K. Substitutions of hydrophobic amino-acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides. J. Mol. Biol. 1992, 228:460-473.
    • (1992) J. Mol. Biol. , vol.228 , pp. 460-473
    • Hilbich, C.1    Kisterswoike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 9
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta-amyloid protein is critical for the seeding of amyloid formation-implications for the pathogenesis of Alzheimer's disease
    • Jarrett J.T., Berger E.P., Lansbury P.T. The carboxy terminus of the beta-amyloid protein is critical for the seeding of amyloid formation-implications for the pathogenesis of Alzheimer's disease. Biochemistry 1993, 32:4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 10
    • 0028980362 scopus 로고
    • The alpha-helical to beta-strand transition in the amino-terminal fragment of the amyloid beta-peptide modulates amyloid formation
    • Soto C., Castano E.M., Frangione B., Inestrosa N.C. The alpha-helical to beta-strand transition in the amino-terminal fragment of the amyloid beta-peptide modulates amyloid formation. J. Biol. Chem. 1995, 270:3063-3067.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3063-3067
    • Soto, C.1    Castano, E.M.2    Frangione, B.3    Inestrosa, N.C.4
  • 12
    • 33746885863 scopus 로고    scopus 로고
    • Potential lead for an Alzheimer drug: a peptide that blocks intermolecular interaction and amyloid beta protein-induced cytotoxicity
    • Kwak J.-W., Kim H.-K., Chae C.-B. Potential lead for an Alzheimer drug: a peptide that blocks intermolecular interaction and amyloid beta protein-induced cytotoxicity. J. Med. Chem. 2006, 49:4813-4817.
    • (2006) J. Med. Chem. , vol.49 , pp. 4813-4817
    • Kwak, J.-W.1    Kim, H.-K.2    Chae, C.-B.3
  • 13
    • 0030600371 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation
    • Soto C., Kindy M.S., Baumann M., Frangione B. Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation. Biochem. Biophys. Res. Commun. 1996, 226:672-680.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 672-680
    • Soto, C.1    Kindy, M.S.2    Baumann, M.3    Frangione, B.4
  • 14
    • 0036257686 scopus 로고    scopus 로고
    • Converting a peptide into a drug: strategies to improve stability and bioavailability
    • Adessi C., Soto C. Converting a peptide into a drug: strategies to improve stability and bioavailability. Curr. Med. Chem. 2002, 9:963-978.
    • (2002) Curr. Med. Chem. , vol.9 , pp. 963-978
    • Adessi, C.1    Soto, C.2
  • 16
    • 33745758083 scopus 로고    scopus 로고
    • Inhibition of protein misfolding and aggregation by small rationally-designed peptides
    • Estrada L.D., Soto C. Inhibition of protein misfolding and aggregation by small rationally-designed peptides. Curr. Pharm. Des. 2006, 12:2557-2567.
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 2557-2567
    • Estrada, L.D.1    Soto, C.2
  • 18
    • 24144437434 scopus 로고    scopus 로고
    • A rapid label-free electrochemical detection and kinetic study of Alzheimer's amyloid beta aggregation
    • Vestergaard M., Kerman K., Saito M., Nagatani N., Takamura Y., Tamiya E. A rapid label-free electrochemical detection and kinetic study of Alzheimer's amyloid beta aggregation. J. Am. Chem. Soc. 2005, 127:11892-11893.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 11892-11893
    • Vestergaard, M.1    Kerman, K.2    Saito, M.3    Nagatani, N.4    Takamura, Y.5    Tamiya, E.6
  • 19
    • 54549095792 scopus 로고    scopus 로고
    • Amyloid-beta detection with saccharide immobilized gold nanoparticle on carbon electrode
    • Chikae M., Fukuda T., Kerman K., Idegami K., Miura Y., Tamiya E. Amyloid-beta detection with saccharide immobilized gold nanoparticle on carbon electrode. Bioelectrochemistry 2008, 74:118-123.
    • (2008) Bioelectrochemistry , vol.74 , pp. 118-123
    • Chikae, M.1    Fukuda, T.2    Kerman, K.3    Idegami, K.4    Miura, Y.5    Tamiya, E.6
  • 20
    • 70649108813 scopus 로고    scopus 로고
    • Electrochemical oxidation of benzothiazole dyes for monitoring amyloid formation related to the Alzheimer's disease
    • Veloso A.J., Hung V.W.S., Sindhu G., Constantinof A., Kerman K. Electrochemical oxidation of benzothiazole dyes for monitoring amyloid formation related to the Alzheimer's disease. Anal. Chem. 2009, 81:9410-9415.
    • (2009) Anal. Chem. , vol.81 , pp. 9410-9415
    • Veloso, A.J.1    Hung, V.W.S.2    Sindhu, G.3    Constantinof, A.4    Kerman, K.5
  • 21
    • 0032855484 scopus 로고    scopus 로고
    • Kinetic analysis of amyloid fibril formation
    • Naiki H., Gejyo F. Kinetic analysis of amyloid fibril formation. Methods Enzymol. 1999, 309:305-318.
    • (1999) Methods Enzymol. , vol.309 , pp. 305-318
    • Naiki, H.1    Gejyo, F.2
  • 22
    • 0031873102 scopus 로고    scopus 로고
    • β-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy
    • Soto C., Sigurdsson E., Morelli L., Kumar R., Castano E., Frangione B. β-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nat. Med. 1998, 4:822-826.
    • (1998) Nat. Med. , vol.4 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.2    Morelli, L.3    Kumar, R.4    Castano, E.5    Frangione, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.