메뉴 건너뛰기




Volumn 377, Issue 5, 2008, Pages 1372-1381

New Strategy for the Generation of Specific d-Peptide Amyloid Inhibitors

Author keywords

amyloid inhibition; amyloid toxicity inhibition; amyloidoses; d peptides; general strategy

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; AMYLOID INHIBITOR; AMYLOID PROTEIN; PEPTIDE LIBRARY; PROTEIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 40949089587     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.01.028     Document Type: Article
Times cited : (31)

References (48)
  • 1
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross C.A., and Poirier M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 10 (2004) S10-S17
    • (2004) Nat. Med. , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 2
    • 4344580888 scopus 로고    scopus 로고
    • Strategies for disease modification in Alzheimer's disease
    • Citron M. Strategies for disease modification in Alzheimer's disease. Nat. Rev. Neurosci. 5 (2004) 677-685
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 677-685
    • Citron, M.1
  • 3
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto C. Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci. 4 (2003) 49-60
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 49-60
    • Soto, C.1
  • 5
    • 0035411641 scopus 로고    scopus 로고
    • Beta-amyloid aggregation inhibitors for the treatment of Alzheimer's disease: dream or reality?
    • Talaga P. Beta-amyloid aggregation inhibitors for the treatment of Alzheimer's disease: dream or reality?. Mini Rev. Med. Chem. 1 (2001) 175-186
    • (2001) Mini Rev. Med. Chem. , vol.1 , pp. 175-186
    • Talaga, P.1
  • 6
    • 0035983921 scopus 로고    scopus 로고
    • The challenge of inhibiting Abeta polymerization
    • LeVine H. The challenge of inhibiting Abeta polymerization. Curr. Med. Chem. 9 (2002) 1121-1133
    • (2002) Curr. Med. Chem. , vol.9 , pp. 1121-1133
    • LeVine, H.1
  • 7
    • 18644384035 scopus 로고    scopus 로고
    • Potent and selective structure-based dibenzofuran inhibitors of transthyretin amyloidogenesis: kinetic stabilization of the native state
    • Petrassi H.M., Johnson S.M., Purkey H.E., Chiang K.P., Walkup T., Jiang X., et al. Potent and selective structure-based dibenzofuran inhibitors of transthyretin amyloidogenesis: kinetic stabilization of the native state. J. Am. Chem. Soc. 127 (2005) 6662-6671
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 6662-6671
    • Petrassi, H.M.1    Johnson, S.M.2    Purkey, H.E.3    Chiang, K.P.4    Walkup, T.5    Jiang, X.6
  • 8
    • 0141632823 scopus 로고    scopus 로고
    • New inhibitors of scrapie-associated prion protein formation in a library of 2000 drugs and natural products
    • Kocisko D.A., Baron G.S., Rubenstein R., Chen J., Kuizon S., and Caughey B. New inhibitors of scrapie-associated prion protein formation in a library of 2000 drugs and natural products. J. Virol. 77 (2003) 10288-10294
    • (2003) J. Virol. , vol.77 , pp. 10288-10294
    • Kocisko, D.A.1    Baron, G.S.2    Rubenstein, R.3    Chen, J.4    Kuizon, S.5    Caughey, B.6
  • 9
    • 0034807861 scopus 로고    scopus 로고
    • Amyloid fibril formation in microwell plates for screening of inhibitors
    • Lin Y.M., Raffen R., Zhou Y., Cassidy C.S., Flavin M.T., and Stevens F.J. Amyloid fibril formation in microwell plates for screening of inhibitors. Amyloid 8 (2001) 182-193
    • (2001) Amyloid , vol.8 , pp. 182-193
    • Lin, Y.M.1    Raffen, R.2    Zhou, Y.3    Cassidy, C.S.4    Flavin, M.T.5    Stevens, F.J.6
  • 10
    • 33749043758 scopus 로고    scopus 로고
    • Peptide model systems for amyloid fiber formation: design strategies and validation methods
    • Esteras-Chopo A., Pastor M.T., and López de la Paz M. Peptide model systems for amyloid fiber formation: design strategies and validation methods. Methods Mol. Biol. 340 (2006) 253-276
    • (2006) Methods Mol. Biol. , vol.340 , pp. 253-276
    • Esteras-Chopo, A.1    Pastor, M.T.2    López de la Paz, M.3
  • 11
    • 0034682788 scopus 로고    scopus 로고
    • Inhibition of toxicity in the beta-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. Inhibition of toxicity in the beta-amyloid peptide fragment β(25-35) using N-methylated derivatives-a general strategy to prevent amyloid formation. J. Biol. Chem. 275 (2000) 25109-25115
    • (2000) J. Biol. Chem. , vol.275 , pp. 25109-25115
    • Hughes, E.1    Burke, R.M.2    Doig, A.J.3
  • 12
    • 0036300750 scopus 로고    scopus 로고
    • Structure-based design and study of non-amyloidogenic, double N-methylated IAPP amyloid core sequences as inhibitors of IAPP amyloid formation and cytotoxicity
    • Kapurniotu A., Schmauder A., and Tenidis K. Structure-based design and study of non-amyloidogenic, double N-methylated IAPP amyloid core sequences as inhibitors of IAPP amyloid formation and cytotoxicity. J. Mol. Biol. 315 (2002) 339-350
    • (2002) J. Mol. Biol. , vol.315 , pp. 339-350
    • Kapurniotu, A.1    Schmauder, A.2    Tenidis, K.3
  • 14
    • 0030600371 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation
    • Soto C., Kindy M.S., Baumann M., and Frangione B. Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation. Biochem. Biophys. Res. Commun. 226 (1996) 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
  • 15
    • 4544388592 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation by peptide analogues modified with alpha-aminoisobutyric acid
    • Gilead S., and Gazit E. Inhibition of amyloid fibril formation by peptide analogues modified with alpha-aminoisobutyric acid. Angew. Chem., Int. Ed. Engl. 43 (2004) 4041-4044
    • (2004) Angew. Chem., Int. Ed. Engl. , vol.43 , pp. 4041-4044
    • Gilead, S.1    Gazit, E.2
  • 16
    • 33646130171 scopus 로고    scopus 로고
    • Inhibition of insulin fibrillogenesis with targeted peptides
    • Gibson T.J., and Murphy R.M. Inhibition of insulin fibrillogenesis with targeted peptides. Protein Sci. 15 (2006) 1133-1141
    • (2006) Protein Sci. , vol.15 , pp. 1133-1141
    • Gibson, T.J.1    Murphy, R.M.2
  • 17
    • 0035800087 scopus 로고    scopus 로고
    • Structure-function relationships for inhibitors of beta-amyloid toxicity containing the recognition sequence KLVFF
    • Lowe T.L., Strzelec A., Kiessling L.L., and Murphy R.M. Structure-function relationships for inhibitors of beta-amyloid toxicity containing the recognition sequence KLVFF. Biochemistry 40 (2001) 7882-7889
    • (2001) Biochemistry , vol.40 , pp. 7882-7889
    • Lowe, T.L.1    Strzelec, A.2    Kiessling, L.L.3    Murphy, R.M.4
  • 18
    • 0036615884 scopus 로고    scopus 로고
    • Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a beta-sheet breaker peptide
    • Permanne B., Adessi C., Saborio G.P., Fraga S., Frossard M.J., Van Dorpe J., et al. Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a beta-sheet breaker peptide. FASEB J. 16 (2002) 860-862
    • (2002) FASEB J. , vol.16 , pp. 860-862
    • Permanne, B.1    Adessi, C.2    Saborio, G.P.3    Fraga, S.4    Frossard, M.J.5    Van Dorpe, J.6
  • 19
    • 0038529679 scopus 로고    scopus 로고
    • Pharmacological profiles of peptide drug candidates for the treatment of Alzheimer's disease
    • Adessi C., Frossard M.J., Boissard C., Fraga S., Bieler S., Ruckle T., et al. Pharmacological profiles of peptide drug candidates for the treatment of Alzheimer's disease. J. Biol. Chem. 278 (2003) 13905-13911
    • (2003) J. Biol. Chem. , vol.278 , pp. 13905-13911
    • Adessi, C.1    Frossard, M.J.2    Boissard, C.3    Fraga, S.4    Bieler, S.5    Ruckle, T.6
  • 20
    • 40949123338 scopus 로고    scopus 로고
    • Soto-Jara, C., Baumann, M. H. & Frangione, B. (2002). Peptides and pharmaceutical compositions thereof for treatment of disorders or diseases associated with abnormal protein folding into amyloid or amyloid-like deposits. US Patent 6462171.
    • Soto-Jara, C., Baumann, M. H. & Frangione, B. (2002). Peptides and pharmaceutical compositions thereof for treatment of disorders or diseases associated with abnormal protein folding into amyloid or amyloid-like deposits. US Patent 6462171.
  • 21
    • 6044240725 scopus 로고    scopus 로고
    • Beta-sheet breaker peptide prevents Abeta-induced spatial memory impairments with partial reduction of amyloid deposits
    • Chacon M.A., Barria M.I., Soto C., and Inestrosa N.C. Beta-sheet breaker peptide prevents Abeta-induced spatial memory impairments with partial reduction of amyloid deposits. Mol. Psychiatry 9 (2004) 953-961
    • (2004) Mol. Psychiatry , vol.9 , pp. 953-961
    • Chacon, M.A.1    Barria, M.I.2    Soto, C.3    Inestrosa, N.C.4
  • 22
    • 40949094578 scopus 로고    scopus 로고
    • Axonyx Announces Milestone Payment from Serono after Initiation of Clinical Trial in Alzheimer's. Press release (April 14, 2003): http://findarticles.com/p/articles/mi_m0EIN/is_2003_April_24/ai_10054655 1
    • Axonyx Announces Milestone Payment from Serono after Initiation of Clinical Trial in Alzheimer's. Press release (April 14, 2003): http://findarticles.com/p/articles/mi_m0EIN/is_2003_April_24/ai_10054655 1
  • 25
    • 0041467577 scopus 로고    scopus 로고
    • Selection of d-amino-acid peptides that bind to Alzheimer's disease amyloid peptide abeta1-42 by mirror image phage display
    • Wiesehan K., Buder K., Linke R.P., Patt S., Stoldt M., Unger E., et al. Selection of d-amino-acid peptides that bind to Alzheimer's disease amyloid peptide abeta1-42 by mirror image phage display. ChemBioChem 4 (2003) 748-753
    • (2003) ChemBioChem , vol.4 , pp. 748-753
    • Wiesehan, K.1    Buder, K.2    Linke, R.P.3    Patt, S.4    Stoldt, M.5    Unger, E.6
  • 26
    • 0031445940 scopus 로고    scopus 로고
    • Mechanism and prevention of neurotoxicity caused by beta-amyloid peptides: relation to Alzheimer's disease
    • Blanchard B.J., Konopka G., Russell M., and Ingram V.M. Mechanism and prevention of neurotoxicity caused by beta-amyloid peptides: relation to Alzheimer's disease. Brain Res. 776 (1997) 40-50
    • (1997) Brain Res. , vol.776 , pp. 40-50
    • Blanchard, B.J.1    Konopka, G.2    Russell, M.3    Ingram, V.M.4
  • 28
    • 11844298976 scopus 로고    scopus 로고
    • Stereospecific amyloid-like fibril formation by a peptide fragment of beta2-microglobulin
    • Wadai H., Yamaguchi K., Takahashi S., Kanno T., Kawai T., Naiki H., and Goto Y. Stereospecific amyloid-like fibril formation by a peptide fragment of beta2-microglobulin. Biochemistry 44 (2005) 157-164
    • (2005) Biochemistry , vol.44 , pp. 157-164
    • Wadai, H.1    Yamaguchi, K.2    Takahashi, S.3    Kanno, T.4    Kawai, T.5    Naiki, H.6    Goto, Y.7
  • 30
    • 28044457195 scopus 로고    scopus 로고
    • The amyloid stretch hypothesis: recruiting proteins toward the dark side
    • Esteras-Chopo A., Serrano L., and López de la Paz M. The amyloid stretch hypothesis: recruiting proteins toward the dark side. Proc. Natl Acad. Sci. USA 102 (2005) 16672-16677
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 16672-16677
    • Esteras-Chopo, A.1    Serrano, L.2    López de la Paz, M.3
  • 31
    • 2442553006 scopus 로고    scopus 로고
    • Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case
    • Ventura S., Zurdo J., Narayanan S., Parreno M., Mangues R., Reif B., et al. Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case. Proc. Natl Acad. Sci. USA 101 (2004) 7258-7263
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7258-7263
    • Ventura, S.1    Zurdo, J.2    Narayanan, S.3    Parreno, M.4    Mangues, R.5    Reif, B.6
  • 32
    • 3242735504 scopus 로고    scopus 로고
    • An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril
    • Ivanova M.I., Sawaya M.R., Gingery M., Attinger A., and Eisenberg D. An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril. Proc. Natl Acad. Sci. USA 101 (2004) 10584-10589
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 10584-10589
    • Ivanova, M.I.1    Sawaya, M.R.2    Gingery, M.3    Attinger, A.4    Eisenberg, D.5
  • 38
    • 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., et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002) 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
  • 39
    • 0035961291 scopus 로고    scopus 로고
    • Pathogenesis, diagnosis and treatment of systemic amyloidosis
    • discussion 210-1
    • Pepys M.B. Pathogenesis, diagnosis and treatment of systemic amyloidosis. Philos. Trans. R. Soc. London, Ser. B 356 (2001) 203-210 discussion 210-1
    • (2001) Philos. Trans. R. Soc. London, Ser. B , vol.356 , pp. 203-210
    • Pepys, M.B.1
  • 40
    • 0027946254 scopus 로고
    • Helix stop and start signals in peptides and proteins. The capping box does not necessarily prevent helix elongation
    • Jimenez M.A., Munoz V., Rico M., and Serrano L. Helix stop and start signals in peptides and proteins. The capping box does not necessarily prevent helix elongation. J. Mol. Biol. 242 (1994) 487-496
    • (1994) J. Mol. Biol. , vol.242 , pp. 487-496
    • Jimenez, M.A.1    Munoz, V.2    Rico, M.3    Serrano, L.4
  • 43
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla A.M., Rousseau F., Schymkowitz J., and Serrano L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 22 (2004) 1302-1306
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 44
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases
    • Pawar A.P., Dubay K.F., Zurdo J., Chiti F., Vendruscolo M., and Dobson C.M. Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 350 (2005) 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
  • 47
    • 24044507958 scopus 로고    scopus 로고
    • Multiple assembly pathways underlie amyloid-beta fibril polymorphisms
    • Goldsbury C., Frey P., Olivieri V., Aebi U., and Muller S.A. Multiple assembly pathways underlie amyloid-beta fibril polymorphisms. J. Mol. Biol. 352 (2005) 282-298
    • (2005) J. Mol. Biol. , vol.352 , pp. 282-298
    • Goldsbury, C.1    Frey, P.2    Olivieri, V.3    Aebi, U.4    Muller, S.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.