메뉴 건너뛰기




Volumn 158, Issue 4, 2009, Pages 1165-1172

Reversal of temperature-induced conformational changes in the amyloid-beta peptide, Aβ40, by the β-sheet breaker peptides 16-23 and 17-24

Author keywords

sheet formation; Alzheimer's disease treatment; Amyloid 1 40; Breaker peptides; Temperature

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; EPITOPE; OCTAPEPTIDE; PROTEINASE K;

EID: 70350131474     PISSN: 00071188     EISSN: 14765381     Source Type: Journal    
DOI: 10.1111/j.1476-5381.2009.00384.x     Document Type: Article
Times cited : (8)

References (43)
  • 2
    • 0032557425 scopus 로고    scopus 로고
    • Dramatic aggregation of Alzheimer abeta by Cu(II) is induced by conditions representing physiological acidosis
    • Atwood CD, Moir RD, Hung X, Scarpa RC, Bacarra NM, Romano DM et al. (1998). Dramatic aggregation of Alzheimer abeta by Cu(II) is induced by conditions representing physiological acidosis. J Biol Chem 273 : 12817 12826.
    • (1998) J Biol Chem , vol.273 , pp. 12817-12826
    • Atwood, C.D.1    Moir, R.D.2    Hung, X.3    Scarpa, R.C.4    Bacarra, N.M.5    Romano, D.M.6
  • 3
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid beta peptides of Alzheimer's disease: Analysis of circular dichroism spectra
    • Barrow CJ, Yasuda A, Kenny PT, Zagorski MG (1992). Solution conformations and aggregational properties of synthetic amyloid beta peptides of Alzheimer's disease: analysis of circular dichroism spectra. J Mol Biol 225 : 1075 1093.
    • (1992) J Mol Biol , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.3    Zagorski, M.G.4
  • 4
    • 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 BM, Cavalli A, Melchiorre C, 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, B.M.3    Cavalli, A.4    Melchiorre, C.5    Andrisano, V.6
  • 5
    • 16344385440 scopus 로고    scopus 로고
    • Oxidative metabolites accelerate Alzheimer's amyloidogenesis by two-step mechanism, eliminating the requirement for nucleation
    • Bieschke J, Zhang Q, Powers WT, Lerner RA, Kelly JW (2005). Oxidative metabolites accelerate Alzheimer's amyloidogenesis by two-step mechanism, eliminating the requirement for nucleation. Biochemistry 44 : 4977 4983.
    • (2005) Biochemistry , vol.44 , pp. 4977-4983
    • Bieschke, J.1    Zhang, Q.2    Powers, W.T.3    Lerner, R.A.4    Kelly, J.W.5
  • 6
    • 0035865539 scopus 로고    scopus 로고
    • Temperature-induced conformational changes in amyloid beta(1-40) peptide investigated by simultaneous FT-IR microspectroscopy with thermal system
    • Chu HL, Lin SY (2001). Temperature-induced conformational changes in amyloid beta(1-40) peptide investigated by simultaneous FT-IR microspectroscopy with thermal system. Biophys Chem 89 : 173 180.
    • (2001) Biophys Chem , vol.89 , pp. 173-180
    • Chu, H.L.1    Lin, S.Y.2
  • 8
    • 33847757861 scopus 로고    scopus 로고
    • Comparative effects of Abeta(1-42)-Al complex from rat and human amyloid on rat endothelial cell cultures
    • Drago D, Folin M, Baiguera S, Tognon G, Ricchelli F, Zatta P (2007). Comparative effects of Abeta(1-42)-Al complex from rat and human amyloid on rat endothelial cell cultures. J Alzheimers Dis 11 : 33 44.
    • (2007) J Alzheimers Dis , vol.11 , pp. 33-44
    • Drago, D.1    Folin, M.2    Baiguera, S.3    Tognon, G.4    Ricchelli, F.5    Zatta, P.6
  • 9
    • 0029866177 scopus 로고    scopus 로고
    • The interaction between apolipoprotein e and Alzheimer's amyloid β-peptide is dependent on β-peptide conformation
    • Golabek AA, Soto C, Vogel T, Wisniewski T (1996). The interaction between apolipoprotein E and Alzheimer's amyloid β-peptide is dependent on β-peptide conformation. J Biol Chem 271 : 10602 10606.
    • (1996) J Biol Chem , vol.271 , pp. 10602-10606
    • Golabek, A.A.1    Soto, C.2    Vogel, T.3    Wisniewski, T.4
  • 10
    • 0033987195 scopus 로고    scopus 로고
    • Temperature-dependent beta-sheet formation in beta-amyloid abeta(1-40) peptide in water: Uncoupling beta-structure folding from aggregation
    • Gursky O, Aleshkov S (2000). Temperature-dependent beta-sheet formation in beta-amyloid abeta(1-40) peptide in water: uncoupling beta-structure folding from aggregation. Biochim Biophys Acta 1476 : 93 102.
    • (2000) Biochim Biophys Acta , vol.1476 , pp. 93-102
    • Gursky, O.1    Aleshkov, S.2
  • 11
    • 0036191829 scopus 로고    scopus 로고
    • Mapping of possible binding sequences of two beta-sheet breaker peptides on beta amyloid peptide of Alzheimer's disease
    • Hetenyi C, Kortvelyesi T, Penke B (2002). Mapping of possible binding sequences of two beta-sheet breaker peptides on beta amyloid peptide of Alzheimer's disease. Bioorg Med Chem 10 : 1587 1593.
    • (2002) Bioorg Med Chem , vol.10 , pp. 1587-1593
    • Hetenyi, C.1    Kortvelyesi, T.2    Penke, B.3
  • 12
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of amyloid βa4 protein of Alzheimer's disease
    • Hilbich C, Kisters WB, Reed J, Masters CL, Beyreuther K (1991). Aggregation and secondary structure of amyloid βA4 protein of Alzheimer's disease. J Mol Biol 218 : 149 163.
    • (1991) J Mol Biol , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters, W.B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 13
    • 0034677660 scopus 로고    scopus 로고
    • Structural studies of soluble oligomers of the Alzheimer β-amyloid peptide
    • Huang JTH, Yang DS, Plaskos NP, Go S, Yip CM, Fraser PE et al. (2000). Structural studies of soluble oligomers of the Alzheimer β-amyloid peptide. J Mol Biol 297 : 73 87.
    • (2000) J Mol Biol , vol.297 , pp. 73-87
    • Huang, J.T.H.1    Yang, D.S.2    Plaskos, N.P.3    Go, S.4    Yip, C.M.5    Fraser, P.E.6
  • 15
    • 0035816709 scopus 로고    scopus 로고
    • Cholesterol-dependent formation of GM1 ganglioside-bound amyloid beta-protein, an endogenous seed for Alzheimer amyloid
    • Kakio A, Nishimoto SI, Yanagisawa K, Kozutsumi Y, Matsuzaki K (2001). Cholesterol-dependent formation of GM1 ganglioside-bound amyloid beta-protein, an endogenous seed for Alzheimer amyloid. J Biol Chem 276 : 24985 24990.
    • (2001) J Biol Chem , vol.276 , pp. 24985-24990
    • Kakio, A.1    Nishimoto, S.I.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 16
    • 0042821622 scopus 로고    scopus 로고
    • Dissolution of beta-2-microglobullin amyloid fibrils by dimethylsulfoxide
    • Kanaoka NH, Hasegawa K, Nakai H, Goto Y (2003). Dissolution of beta-2-microglobullin amyloid fibrils by dimethylsulfoxide. J Biochem 134 : 159 164.
    • (2003) J Biochem , vol.134 , pp. 159-164
    • Kanaoka, N.H.1    Hasegawa, K.2    Nakai, H.3    Goto, Y.4
  • 17
    • 0037375473 scopus 로고    scopus 로고
    • C-terminal fragments of amyloid-β peptide cause cholinergic axonal degeneration by a toxic effect rather than by physical injury in the nondemented human brain
    • Kasa P, Papp H, Zombori J, Mayer P, Checler F (2003). C-terminal fragments of amyloid-β peptide cause cholinergic axonal degeneration by a toxic effect rather than by physical injury in the nondemented human brain. Neurochem Res 28 : 493 498.
    • (2003) Neurochem Res , vol.28 , pp. 493-498
    • Kasa, P.1    Papp, H.2    Zombori, J.3    Mayer, P.4    Checler, F.5
  • 18
    • 0025911018 scopus 로고
    • Advances in Alzheimer's disease
    • Katzman R, Saitoh T (1991). Advances in Alzheimer's disease. FASEB J 5 : 278 286.
    • (1991) FASEB J , vol.5 , pp. 278-286
    • Katzman, R.1    Saitoh, T.2
  • 19
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid beta protein forms ion channels: Implications for Alzheimer's disease pathophysiology
    • Lin H, Bhatia R, Lal R (2001). Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology. FASEB J 15 : 2433 2444.
    • (2001) FASEB J , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 20
    • 0036128434 scopus 로고    scopus 로고
    • Pressure-induced transformation of alpha-helix to beta-sheet in the secondary structures of amyloid beta (1-40) peptide exacerbated by temperature
    • Lin SY, Chu HL, Wie YS (2002). Pressure-induced transformation of alpha-helix to beta-sheet in the secondary structures of amyloid beta (1-40) peptide exacerbated by temperature. J Biomol Struct Dyn 9 : 619 625.
    • (2002) J Biomol Struct Dyn , vol.9 , pp. 619-625
    • Lin, S.Y.1    Chu, H.L.2    Wie, Y.S.3
  • 21
    • 0037319127 scopus 로고    scopus 로고
    • Secondary conformations and temperature effect on structural transformation of amyloid beta(1-28), (1-40) and (1-42) peptides
    • Lin SY, Chu HL, Wie YS (2003). Secondary conformations and temperature effect on structural transformation of amyloid beta(1-28), (1-40) and (1-42) peptides. J Biomol Struct Dyn 20 : 595 601.
    • (2003) J Biomol Struct Dyn , vol.20 , pp. 595-601
    • Lin, S.Y.1    Chu, H.L.2    Wie, Y.S.3
  • 22
    • 0346099098 scopus 로고    scopus 로고
    • Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation
    • Lui R, MaAllister C, Lyubchenko Y, Sierks MR (2004). Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation. J Neurosci Res 75 : 162 171.
    • (2004) J Neurosci Res , vol.75 , pp. 162-171
    • Lui, R.1    Maallister, C.2    Lyubchenko, Y.3    Sierks, M.R.4
  • 23
    • 0036471358 scopus 로고    scopus 로고
    • A pH-dependent conformational transition of Aβ peptide and physicochemical properties of the conformers in the glial cell
    • Matsunaga Y, Saito N, Fuji A, Yokotani J, Takakura T, Nishimura T et al. (2002). A pH-dependent conformational transition of Aβ peptide and physicochemical properties of the conformers in the glial cell. Biochem J 361 : 547 556.
    • (2002) Biochem J , vol.361 , pp. 547-556
    • Matsunaga, Y.1    Saito, N.2    Fuji, A.3    Yokotani, J.4    Takakura, T.5    Nishimura, T.6
  • 24
    • 2642557773 scopus 로고    scopus 로고
    • Eight-residue Aβ peptides inhibit the aggregation and enzymatic activity of Aβ42
    • Matsunaga Y, Fuji A, Awasthia A, Yokotanib J, Takakura T, Yamada T (2004). Eight-residue Aβ peptides inhibit the aggregation and enzymatic activity of Aβ42. Regul Pept 120 : 227 236.
    • (2004) Regul Pept , vol.120 , pp. 227-236
    • Matsunaga, Y.1    Fuji, A.2    Awasthia, A.3    Yokotanib, J.4    Takakura, T.5    Yamada, T.6
  • 26
    • 0033596944 scopus 로고    scopus 로고
    • Recognition sequence design for peptidyl modulators of beta-amyloid aggregation and toxicity
    • Pallitto MM, Ghanta J, Heinzelman P, Kiessling LL, Murphy RM (1999). Recognition sequence design for peptidyl modulators of beta-amyloid aggregation and toxicity. Biochemistry 38 : 3570 3578.
    • (1999) Biochemistry , vol.38 , pp. 3570-3578
    • Pallitto, M.M.1    Ghanta, J.2    Heinzelman, P.3    Kiessling, L.L.4    Murphy, R.M.5
  • 27
    • 0036050867 scopus 로고    scopus 로고
    • Are β-sheet breaker peptides dissolving the therapeutic problem of Alzheimer's disease?
    • Permanne B, Adessi C, Fraga S, Frossard MJ, Saborio GP, Soto C (2002a). Are β-sheet breaker peptides dissolving the therapeutic problem of Alzheimer's disease? J Neural Transm 62 : 293 301.
    • (2002) J Neural Transm , vol.62 , pp. 293-301
    • Permanne, B.1    Adessi, C.2    Fraga, S.3    Frossard, M.J.4    Saborio, G.P.5    Soto, C.6
  • 28
    • 0036615884 scopus 로고    scopus 로고
    • Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with β-sheet breaker peptide
    • Permanne B, Adessi C, Saborio GP, Fraga S, Frossard MJ, Dorpe JV et al. (2002b). Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with β-sheet breaker peptide. FASEB J 16 : 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    Dorpe, J.V.6
  • 29
    • 0344255649 scopus 로고    scopus 로고
    • Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide
    • Petkova AT, Buntkowsky G, Dyda F, Leapman RD, Yau WM, Tycko R (2004). Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide. J Mol Biol 335 : 247 260.
    • (2004) J Mol Biol , vol.335 , pp. 247-260
    • Petkova, A.T.1    Buntkowsky, G.2    Dyda, F.3    Leapman, R.D.4    Yau, W.M.5    Tycko, R.6
  • 30
    • 0041817542 scopus 로고    scopus 로고
    • The amyloid beta peptide(abeta1-40) is thermodynamically soluble at physiological concentrations
    • Sengupta P, Garai K, Sahoo B, Shi Y, Callaway DJ, Maiti S (2003). The amyloid beta peptide(abeta1-40) is thermodynamically soluble at physiological concentrations. Biochemistry 42 : 10506 10513.
    • (2003) Biochemistry , vol.42 , pp. 10506-10513
    • Sengupta, P.1    Garai, K.2    Sahoo, B.3    Shi, Y.4    Callaway, D.J.5    Maiti, S.6
  • 31
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar GM, Li S, Mehta TH, Garcia A, Hepardson NE, Smith I et al. (2008). Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med 14 : 837 842.
    • (2008) Nat Med , vol.14 , pp. 837-842
    • Shankar, G.M.1    Li, S.2    Mehta, T.H.3    Garcia, A.4    Hepardson, N.E.5    Smith, I.6
  • 32
    • 0029157531 scopus 로고
    • Solvent effects on self-assembly of β-amyloid peptide
    • Shen CL, Murphy RM (1995). Solvent effects on self-assembly of β-amyloid peptide. Biophys J 69 : 640 651.
    • (1995) Biophys J , vol.69 , pp. 640-651
    • Shen, C.L.1    Murphy, R.M.2
  • 35
    • 0036944135 scopus 로고    scopus 로고
    • Postischemic hyperthermia induces Alzheimer-like pathology in the rat brain
    • Sinigaglia-Coimbra R, Cavalheiro EA, Coimbra CG (2002). Postischemic hyperthermia induces Alzheimer-like pathology in the rat brain. Acta Neuropathol 103 : 444 452.
    • (2002) Acta Neuropathol , vol.103 , pp. 444-452
    • Sinigaglia-Coimbra, R.1    Cavalheiro, E.A.2    Coimbra, C.G.3
  • 36
    • 0030600371 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation
    • Soto C, Kidney MS, Baumann M, Frangione B (1996). Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation. Biochem Biohys Res Commun 226 : 672 680.
    • (1996) Biochem Biohys Res Commun , vol.226 , pp. 672-680
    • Soto, C.1    Kidney, M.S.2    Baumann, M.3    Frangione, B.4
  • 37
    • 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 EM, Morelli L, Kumar RA, Castano EM, Frangione B (1998). β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nat Med 4 : 822 826.
    • (1998) Nat Med , vol.4 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, R.A.4    Castano, E.M.5    Frangione, B.6
  • 38
    • 0034486603 scopus 로고    scopus 로고
    • Inhibiting the conversion of soluble amyloid-β peptide into abnormally folded amyloidogenic intermediates: Relevance for Alzheimer's disease therapy
    • Soto C, Saborio GP, Permanne B (2000). Inhibiting the conversion of soluble amyloid-β peptide into abnormally folded amyloidogenic intermediates: relevance for Alzheimer's disease therapy. Acta Neurol Scand 176 : 90 95.
    • (2000) Acta Neurol Scand , vol.176 , pp. 90-95
    • Soto, C.1    Saborio, G.P.2    Permanne, B.3
  • 39
    • 0028168336 scopus 로고
    • Amyloid-β aggregation: Selective inhibition of aggregation in mixtures of amyloid with different chain lenghts
    • Synder SW, Ladror US, Wade WS, Wang GT, Barrett LW, Matayoshi ED et al. (1994). Amyloid-β aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lenghts. Biophys J 67 : 1216 1228.
    • (1994) Biophys J , vol.67 , pp. 1216-1228
    • Synder, S.W.1    Ladror, U.S.2    Wade, W.S.3    Wang, G.T.4    Barrett, L.W.5    Matayoshi, E.D.6
  • 42
    • 33644818046 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of Aβ(1-40) amyloid fibril stability
    • DOI 10.1016/j.jmb.2006.01.041, PII S0022283606000696
    • Williams AD, Shivaprasad S, Ronald WR (2006). Alanine scanning mutagenesis of Aβ(1-40) amyloid fibril stability. J Mol Biol 357 : 1283 1294. (Pubitemid 43357988)
    • (2006) Journal of Molecular Biology , vol.357 , Issue.4 , pp. 1283-1294
    • Williams, A.D.1    Shivaprasad, S.2    Wetzel, R.3
  • 43
    • 0036451728 scopus 로고    scopus 로고
    • Cholesterol-dependent aggregation of amyloid beta-protein
    • Yanagisawa K, Matsuzaki K (2002). Cholesterol-dependent aggregation of amyloid beta-protein. Ann N Y Acad Sci 977 : 384 986.
    • (2002) Ann N y Acad Sci , vol.977 , pp. 384-986
    • Yanagisawa, K.1    Matsuzaki, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.