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Volumn 74, Issue 3, 2009, Pages 224-233

A new series of 1,3-dihidro-imidazo[1,5-c]thiazole-5,7-dione derivatives: Synthesis and interaction with Aβ(25-35) amyloid peptide

Author keywords

amyloid peptide; A (25 35); Fibril modulators; Interaction

Indexed keywords

ALIPHATIC AMINE; AMYLOID BETA PROTEIN[25-35]; THIAZOLE DERIVATIVE;

EID: 68949199661     PISSN: 17470277     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2009.00853.x     Document Type: Article
Times cited : (12)

References (49)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe D.J. (2001) Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 81 : 741 766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 2
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's disease
    • Walsh D., Selkoe D. (2004) Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron 44 : 181 193.
    • (2004) Neuron , vol.44 , pp. 181-193
    • Walsh, D.1    Selkoe, D.2
  • 3
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • Sipe J.D., Cohen A.S. (2000) Review: history of the amyloid fibril. J Struct Biol 130 : 88 98.
    • (2000) J Struct Biol , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 4
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J., Selkoe D.J. (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 : 353 356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 5
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe D.J. (1999) Translating cell biology into therapeutic advances in Alzheimer's disease. Nature 399 : A23 A31.
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 7
    • 0022547855 scopus 로고
    • X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation
    • Kirschner D.A., Abraham C., Selkoe D.J. (1986) X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation. Proc Natl Acad Sci USA 83 : 503 507.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 503-507
    • Kirschner, D.A.1    Abraham, C.2    Selkoe, D.J.3
  • 8
    • 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. (1995) The alpha-helical to beta-strand transition in the amino-terminal fragment of the amyloid beta-peptide modulates amyloid formation. J Biol Chem 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
  • 9
    • 32344451179 scopus 로고    scopus 로고
    • The alpha-to-beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: A step by step conformational analysis suggests the location of beta conformation seeding
    • Tomaselli S., Esposito V., Vangone P., van Nuland N.A., Bonvin A.M., Guerrini R., Tancredi T., Temussi P.A., Picone D. (2006) The alpha-to-beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of beta conformation seeding. Chembiochem 7 : 257 267.
    • (2006) Chembiochem , vol.7 , pp. 257-267
    • Tomaselli, S.1    Esposito, V.2    Vangone, P.3    Van Nuland, N.A.4    Bonvin, A.M.5    Guerrini, R.6    Tancredi, T.7    Temussi, P.A.8    Picone, D.9
  • 10
    • 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., 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
  • 11
    • 1842482905 scopus 로고    scopus 로고
    • Pharmaceutical strategies against amyloidosis: Old and new drugs in targeting a 'protein misfolding disease'
    • De Lorenzi E., Giorgetti S., Grossi S., Merlini G., Caccialanza G., Bellotti V. (2004) Pharmaceutical strategies against amyloidosis: old and new drugs in targeting a 'protein misfolding disease'. Curr Med Chem 11 : 1065 1084.
    • (2004) Curr Med Chem , vol.11 , pp. 1065-1084
    • De Lorenzi, E.1    Giorgetti, S.2    Grossi, S.3    Merlini, G.4    Caccialanza, G.5    Bellotti, V.6
  • 12
    • 15944401392 scopus 로고    scopus 로고
    • Amyloid inhibitors and beta-sheet breakers
    • Soto C., Estrada L. (2005) Amyloid inhibitors and beta-sheet breakers. Subcell Biochem 38 : 351 364.
    • (2005) Subcell Biochem , vol.38 , pp. 351-364
    • Soto, C.1    Estrada, L.2
  • 13
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin M.R., Wells J.A. (2004) Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat Rev Drug Discov 3 : 301 317.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 15
    • 48849104834 scopus 로고    scopus 로고
    • Molecules that target beta-amyloid
    • Stains C.I., Mondal K., Ghosh I. (2007) Molecules that target beta-amyloid. ChemMedChem 2 : 1674 1692.
    • (2007) ChemMedChem , vol.2 , pp. 1674-1692
    • Stains, C.I.1    Mondal, K.2    Ghosh, I.3
  • 18
    • 0028179865 scopus 로고
    • Alzheimer beta-amyloid peptide 25-35: Electrostatic interactions with phospholipid membranes
    • Terzi E., Holzemann G., Seelig J. (1994) Alzheimer beta-amyloid peptide 25-35: electrostatic interactions with phospholipid membranes. Biochemistry 33 : 7434 7441.
    • (1994) Biochemistry , vol.33 , pp. 7434-7441
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 19
    • 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., Cotman C.W. (1993) Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state. J Neurosci 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    Cotman, C.W.5
  • 20
    • 0028981219 scopus 로고
    • Structure-activity analyses of beta-amyloid peptides: Contributions of the beta 25-35 region to aggregation and neurotoxicity
    • Pike C.J., Walencewicz-Wasserman A.J., Kosmoski J., Cribbs D.H., Glabe C.G., Cotman C.W. (1995) Structure-activity analyses of beta-amyloid peptides: contributions of the beta 25-35 region to aggregation and neurotoxicity. J Neurochem 64 : 253 265.
    • (1995) J Neurochem , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 23
    • 0032855482 scopus 로고    scopus 로고
    • Methodological and chemical factors affecting amyloid beta peptide amyloidogenicity
    • Zagorski M.G., Yang J., Shao H., Ma K., Zeng H., Hong A. (1999) Methodological and chemical factors affecting amyloid beta peptide amyloidogenicity. Methods Enzymol 309 : 189 204.
    • (1999) Methods Enzymol , vol.309 , pp. 189-204
    • Zagorski, M.G.1    Yang, J.2    Shao, H.3    Ma, K.4    Zeng, H.5    Hong, A.6
  • 24
    • 0030030956 scopus 로고    scopus 로고
    • First-order kinetic model of Alzheimer's beta-amyloid fibril extension in vitro
    • Naiki H., Nakakuki K. (1996) First-order kinetic model of Alzheimer's beta-amyloid fibril extension in vitro. Lab Invest 74 : 374 383.
    • (1996) Lab Invest , vol.74 , pp. 374-383
    • Naiki, H.1    Nakakuki, K.2
  • 25
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore L., Wallace B. (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 32 : W668 W673.
    • (2004) Nucleic Acids Res , vol.32
    • Whitmore, L.1    Wallace, B.2
  • 26
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A., Davis D. (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J Magn Reson 65 : 355 360.
    • (1985) J Magn Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.2
  • 27
    • 84915716471 scopus 로고
    • Elucidation of cross-relaxation in liquids by two-dimensional NMR
    • Macura S., Ernst R. (1980) Elucidation of cross-relaxation in liquids by two-dimensional NMR. Mol Phys 41 : 95 117.
    • (1980) Mol Phys , vol.41 , pp. 95-117
    • MacUra, S.1    Ernst, R.2
  • 28
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener J., Meier B., Bachmann P., Ernst R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy. J Chem Phys 71 : 4546.
    • (1979) J Chem Phys , vol.71 , pp. 4546
    • Jeener, J.1    Meier, B.2    Bachmann, P.3    Ernst, R.4
  • 29
    • 0004757060 scopus 로고    scopus 로고
    • San Francisco: University of California
    • Goddard T., Kneller D. (2004) SPARKY 3. San Francisco : University of California.
    • (2004) SPARKY , vol.3
    • Goddard, T.1    Kneller, D.2
  • 30
    • 0037571112 scopus 로고    scopus 로고
    • Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94
    • Halgren T. (1996) Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94. J Comput Chem 17 : 490 519.
    • (1996) J Comput Chem , vol.17 , pp. 490-519
    • Halgren, T.1
  • 32
    • 84986513567 scopus 로고
    • Determining atom-centered monopoles from molecular electrostatic potentials. The need for high sampling density in formamide conformational analysis
    • Breneman C., Wiberg K. (1990) Determining atom-centered monopoles from molecular electrostatic potentials. The need for high sampling density in formamide conformational analysis. J Comput Chem 11 : 361 373.
    • (1990) J Comput Chem , vol.11 , pp. 361-373
    • Breneman, C.1    Wiberg, K.2
  • 33
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris G., Goodsell D., Halliday R., Huey R., Hart W., Belew R., Olson A. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J Comput Chem 19 : 1639 1662.
    • (1998) J Comput Chem , vol.19 , pp. 1639-1662
    • Morris, G.1    Goodsell, D.2    Halliday, R.3    Huey, R.4    Hart, W.5    Belew, R.6    Olson, A.7
  • 34
    • 0033397980 scopus 로고    scopus 로고
    • Python: A programming language for software integration and development
    • Sanner M. (1999) Python: a programming language for software integration and development. J Mol Graph Model 17 : 57 61.
    • (1999) J Mol Graph Model , vol.17 , pp. 57-61
    • Sanner, M.1
  • 36
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • Sanner M., Olson A., Spehner J. (1996) Reduced surface: an efficient way to compute molecular surfaces. Biopolymers 38 : 305 320.
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.1    Olson, A.2    Spehner, J.3
  • 37
    • 0028030236 scopus 로고
    • Diels-Alder reactions of 2-azadienes derived from cysteine and serine methyl esters and aldehydes
    • Gilchrist T., Rocha Gonsalves A., Pinho e Melo T. (1994) Diels-Alder reactions of 2-azadienes derived from cysteine and serine methyl esters and aldehydes. Tetrahedron 50 : 13709 13724.
    • (1994) Tetrahedron , vol.50 , pp. 13709-13724
    • Gilchrist, T.1    Rocha Gonsalves, A.2    Pinho E Melo, T.3
  • 38
    • 33751157494 scopus 로고
    • A safe and efficient method for preparation of N,N′-unsymmetrically disubstituted ureas utilizing triphosgene
    • Majer P., Randad R. (1994) A safe and efficient method for preparation of N,N′-unsymmetrically disubstituted ureas utilizing triphosgene. J Org Chem 59 : 1937 1938.
    • (1994) J Org Chem , vol.59 , pp. 1937-1938
    • Majer, P.1    Randad, R.2
  • 39
    • 0028901827 scopus 로고
    • Solid-phase synthesis of 'small' organic molecules based on thiazolidine scaffold
    • Pátek M., Drake B., Lebl M. (1995) Solid-phase synthesis of 'small' organic molecules based on thiazolidine scaffold. Tetrahedron Lett 36 : 2227 2230.
    • (1995) Tetrahedron Lett , vol.36 , pp. 2227-2230
    • Pátek, M.1    Drake, B.2    Lebl, M.3
  • 40
    • 0031896694 scopus 로고    scopus 로고
    • Diastereo-and regioisomeric bicyclic thiohydantoins from chiral 1,3-thiazolidine-2,4-dicarboxylic acids
    • Miskolczi I., Zekany A., Rantal F., Linden A., Kover K., Gyorgydeak Z. (1998) Diastereo-and regioisomeric bicyclic thiohydantoins from chiral 1,3-thiazolidine-2,4-dicarboxylic acids. Helv Chim Acta 81 : 744 753.
    • (1998) Helv Chim Acta , vol.81 , pp. 744-753
    • Miskolczi, I.1    Zekany, A.2    Rantal, F.3    Linden, A.4    Kover, K.5    Gyorgydeak, Z.6
  • 41
    • 0001736119 scopus 로고
    • An improved method for two-dimensional heteronuclear relayed-coherence- transfer NMR spectroscopy
    • Bax A., Davis D., Sarkar S. (1985) An improved method for two-dimensional heteronuclear relayed-coherence-transfer NMR spectroscopy. J Magn Reson 63 : 230 234.
    • (1985) J Magn Reson , vol.63 , pp. 230-234
    • Bax, A.1    Davis, D.2    Sarkar, S.3
  • 42
    • 44949276869 scopus 로고
    • Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy
    • Palmer A., Cavanagh J., Wright P., Rance M. (1991) Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy. J Magn Reson 93 : 151 170.
    • (1991) J Magn Reson , vol.93 , pp. 151-170
    • Palmer, A.1    Cavanagh, J.2    Wright, P.3    Rance, M.4
  • 45
    • 0030600371 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation
    • Soto C., Kindy M., Baumann M., Frangione B. (1996) Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation. Biochem Biophys Res Commun 226 : 672 680.
    • (1996) Biochem Biophys Res Commun , vol.226 , pp. 672-680
    • Soto, C.1    Kindy, M.2    Baumann, M.3    Frangione, B.4
  • 46
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin
    • LeVine H. (1999) Quantification of beta-sheet amyloid fibril structures with thioflavin. Methods Enzymol 309 : 274 284.
    • (1999) Methods Enzymol , vol.309 , pp. 274-284
    • Levine, H.1
  • 47
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease ß-amyloid peptides: Detection of amyloid aggregation in solution
    • Levine H III. (1993) Thioflavine T interaction with synthetic Alzheimer's disease ß-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci 2 : 404 410.
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • Levine III, H.1
  • 48
    • 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., 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
  • 49
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe C. (2008) Structural classification of toxic amyloid oligomers. J Biol Chem 283 : 29639 29643.
    • (2008) J Biol Chem , vol.283 , pp. 29639-29643
    • Glabe, C.1


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