메뉴 건너뛰기




Volumn 10, Issue 5, 2007, Pages 533-539

Peptide inhibitors of β-amyloid aggregation

Author keywords

Sheet; Alzheimer's disease; Drug; Fibril; Peptidomimetic

Indexed keywords

4' IODOESORUBICIN; AMYLOID BETA PROTEIN; ANTHRACYCLINE; BETA CYCLODEXTRIN; CHOLINESTERASE INHIBITOR; CHOLYL LEUCYLVALYLPHENYLALANYLPHENYLALANYLALANYL; COLLAGEN TYPE 4; DAUNORUBICIN; DEXTRO[(METHYLLEUCINE)VALYLPHENYLALANYLPHENYLALANYLLEUCYL]AMIDE; DEXTRO[[R CYCLOHEXYLGLYCINE]Y(R CYCLOHEXYLGLYCINE)(R CYCLOHEXYLGLYCINE)[N METHYLLEUCINE]]AMIDE; DONEPEZIL; GLYCOSAMINOGLYCAN; GLYCYLVALYLVALYLISOLEUCYLALANYL AMIDE; LEUCYLPROLYLPHENYLALANYLPHENYLALANYLASPARTYL; LYSYLLEUCYLVALYLPHENYLALANYLPHENYLALANYL; LYSYLLEUCYLVALYLPHENYLALANYLPHENYLALANYLGLUTAMYLGLUTAMYLGLUTAMYLGLUTAMYL; LYSYLLEUCYLVALYLPHENYLALANYLPHENYLALANYLLYSYLLYSYLLYSYLLYSYL; LYSYLLEUCYLVALYLPHENYLALANYLPHENYLALANYLLYSYLLYSYLLYSYLLYSYLLYSYLLYSYL; LYSYLLEUCYLVALYLPHENYLALANYLPHENYLALANYLSERYLSERYLSERYLSERYL; MELATONIN; MEMANTINE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR BLOCKING AGENT; NONSTEROID ANTIINFLAMMATORY AGENT; PENTAPEPTIDE; PEPTIDE INHIBITOR; PORPHYRIN; PPI 1019; PPI 368; PROTEIN INHIBITOR; RIFAMPICIN; SEN 304; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALYLGLYCYLGLYCYLVALYLVALYL;

EID: 34548410504     PISSN: 13676733     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (72)

References (50)
  • 1
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM: Protein misfolding, evolution and disease. Trends Biochem Sci (1999) 24(9):329-332.
    • (1999) Trends Biochem Sci , vol.24 , Issue.9 , pp. 329-332
    • Dobson, C.M.1
  • 2
    • 0026086869 scopus 로고
    • Molecular studies in Alzheimer's disease
    • Holtzman DM, Mobley WC: Molecular studies in Alzheimer's disease. Trends Biochem Sci (1991) 16(4):140-144.
    • (1991) Trends Biochem Sci , vol.16 , Issue.4 , pp. 140-144
    • Holtzman, D.M.1    Mobley, W.C.2
  • 3
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe DJ: Translating cell biology into therapeutic advances in Alzheimer's disease. Nature (1999) 399(6738 Suppl):A23-A31.
    • (1999) Nature , vol.399 , Issue.6738 SUPPL.
    • Selkoe, D.J.1
  • 4
    • 0036827161 scopus 로고    scopus 로고
    • Aβ as a bioflocculant: Implications for the amyloid hypothesis of Alzheimer's disease
    • Robinson S, Bishop GM: Aβ as a bioflocculant: Implications for the amyloid hypothesis of Alzheimer's disease. Neurobiol Aging (2002) 23(6):1051-1072.
    • (2002) Neurobiol Aging , vol.23 , Issue.6 , pp. 1051-1072
    • Robinson, S.1    Bishop, G.M.2
  • 5
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Aβ oligomers: The solution to an Alzheimer's disease conundrum?
    • Klein WL, Krafft GA, Finch CE: Targeting small Aβ oligomers: The solution to an Alzheimer's disease conundrum?Trends Neurosci (2001) 24(4):219-224.
    • (2001) Trends Neurosci , vol.24 , Issue.4 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 7
    • 33645038471 scopus 로고    scopus 로고
    • Lesné S, Kosh MT, Kotilinek L, Kayed R, Glabe CG, Yang A, Gallagher M, Ashe KH: A specific amyloid-β protein assembly in the brain impairs memory. Nature (2006) 440(7082):352-357. •• Identification of Aβ dodecamers as the primary toxic species in transgenic mice.
    • Lesné S, Kosh MT, Kotilinek L, Kayed R, Glabe CG, Yang A, Gallagher M, Ashe KH: A specific amyloid-β protein assembly in the brain impairs memory. Nature (2006) 440(7082):352-357. •• Identification of Aβ dodecamers as the primary toxic species in transgenic mice.
  • 8
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurondegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • Haass C, Selkoe DJ: Soluble protein oligomers in neurondegeneration: Lessons from the Alzheimer's amyloid β-peptide. Nat Rev Mol Cell Biol (2007) 8(2):101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 9
    • 34248190279 scopus 로고    scopus 로고
    • Walsh DM, Selkoe DJ: Aβ oligomers - a decade of discovery. J Neurochem (2007) 101(5):1172-1184. • Highly readable review of current thinking on the importance of Aβ oligomers.
    • Walsh DM, Selkoe DJ: Aβ oligomers - a decade of discovery. J Neurochem (2007) 101(5):1172-1184. • Highly readable review of current thinking on the importance of Aβ oligomers.
  • 11
    • 33750455150 scopus 로고    scopus 로고
    • Willem M, Garratt AN, Novak B, Citron M, Kaufmann S, Rittger A, DeStrooper B, Saftig P, Birchmeier C, Haass C: Control of peripheral nerve myelination by the β-secretase BACE1. Science (2006) 314(5799):664-666. •• BACE1 is demonstrated to be involved with myelination and correct bundling of axons by Schwann cells, suggesting that its inhibition may not be a good strategy for the treatment of AD.
    • Willem M, Garratt AN, Novak B, Citron M, Kaufmann S, Rittger A, DeStrooper B, Saftig P, Birchmeier C, Haass C: Control of peripheral nerve myelination by the β-secretase BACE1. Science (2006) 314(5799):664-666. •• BACE1 is demonstrated to be involved with myelination and correct bundling of axons by Schwann cells, suggesting that its inhibition may not be a good strategy for the treatment of AD.
  • 12
    • 33847021476 scopus 로고    scopus 로고
    • Presenilin diversifies its portfolio
    • Parks AL, Curtis D: Presenilin diversifies its portfolio. Trends Genet (2007) 23(3):140-150.
    • (2007) Trends Genet , vol.23 , Issue.3 , pp. 140-150
    • Parks, A.L.1    Curtis, D.2
  • 13
    • 0033536163 scopus 로고    scopus 로고
    • Schenk D, Barbour R, Dunn W, Gordon G, Grajeda H, Guido T, Hu K, Huang J, Johnson-Wood K, Khan K, Kholodenko D et al: Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature (1999) 400(6740):173-177. •• This study demonstrates that vaccination with Aβ can prevent AD pathology in a transgenic mouse.
    • Schenk D, Barbour R, Dunn W, Gordon G, Grajeda H, Guido T, Hu K, Huang J, Johnson-Wood K, Khan K, Kholodenko D et al: Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature (1999) 400(6740):173-177. •• This study demonstrates that vaccination with Aβ can prevent AD pathology in a transgenic mouse.
  • 14
    • 0037393454 scopus 로고    scopus 로고
    • Nicoll JA, Wilkinson D, Holmes C, Steart P, Markham H, Weller RO: Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: A case report. Nat Med (2003) 9(4):448-452. • Results of Aβ vaccination in a human trial.
    • Nicoll JA, Wilkinson D, Holmes C, Steart P, Markham H, Weller RO: Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: A case report. Nat Med (2003) 9(4):448-452. • Results of Aβ vaccination in a human trial.
  • 15
    • 33847339301 scopus 로고    scopus 로고
    • NSAIDs and Alzheimer disease: Epidemiological, animal model and clinical studies
    • McGeer PL, McGeer EG: NSAIDs and Alzheimer disease: Epidemiological, animal model and clinical studies. Neurobiol Aging (2007) 28(5):639-647.
    • (2007) Neurobiol Aging , vol.28 , Issue.5 , pp. 639-647
    • McGeer, P.L.1    McGeer, E.G.2
  • 16
    • 33745727582 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease
    • Chauhan V, Chauhan A: Oxidative stress in Alzheimer's disease. Pathophysiology (2006) 13(3):195-208.
    • (2006) Pathophysiology , vol.13 , Issue.3 , pp. 195-208
    • Chauhan, V.1    Chauhan, A.2
  • 17
    • 23044449398 scopus 로고    scopus 로고
    • Quist A, Doudevski I, Lin H, Azimova R, Ng D, Frangione B, Kagan B, Ghiso J, Lal R: Amyloid ion channels: A common structural link for protein-misfolding disease. Proc Nat Acad Sci USA (2005) 102(30):10427-10432. •• Ion channel formation is demonstrated to be associated with a wide range of amyloidogenic peptides and proteins.
    • Quist A, Doudevski I, Lin H, Azimova R, Ng D, Frangione B, Kagan B, Ghiso J, Lal R: Amyloid ion channels: A common structural link for protein-misfolding disease. Proc Nat Acad Sci USA (2005) 102(30):10427-10432. •• Ion channel formation is demonstrated to be associated with a wide range of amyloidogenic peptides and proteins.
  • 18
    • 0036860349 scopus 로고    scopus 로고
    • Metal complexing agents as therapies for Alzheimer's disease
    • Bush AI: Metal complexing agents as therapies for Alzheimer's disease. Neurobiol Aging (2002) 23(6):1031-1038.
    • (2002) Neurobiol Aging , vol.23 , Issue.6 , pp. 1031-1038
    • Bush, A.I.1
  • 19
    • 0031197194 scopus 로고    scopus 로고
    • Inhibition of amyloid formation: A strategy to delay the onset of Alzheimer's disease
    • Lansbury PT: Inhibition of amyloid formation: A strategy to delay the onset of Alzheimer's disease. Curr Opin Chem Biol (1997) 1(2):260-267.
    • (1997) Curr Opin Chem Biol , vol.1 , Issue.2 , pp. 260-267
    • Lansbury, P.T.1
  • 22
    • 0028176698 scopus 로고
    • β-Cyclodextrin interacts with the Alzheimer amyloid β-A4 peptide
    • Camilleri P, Haskins NJ, Howlett DR: β-Cyclodextrin interacts with the Alzheimer amyloid β-A4 peptide. FEBS Lett (1994) 341(2-3):256-258.
    • (1994) FEBS Lett , vol.341 , Issue.2-3 , pp. 256-258
    • Camilleri, P.1    Haskins, N.J.2    Howlett, D.R.3
  • 23
    • 0030778396 scopus 로고    scopus 로고
    • Hemin and related porphyrins inhibit β-amyloid aggregation
    • Howlett D, Cutler P, Heales S, Camilleri P: Hemin and related porphyrins inhibit β-amyloid aggregation. FEBS Lett (1997) 417(2):249-251.
    • (1997) FEBS Lett , vol.417 , Issue.2 , pp. 249-251
    • Howlett, D.1    Cutler, P.2    Heales, S.3    Camilleri, P.4
  • 26
    • 0029863551 scopus 로고    scopus 로고
    • Inhibition of amyloid β protein aggregation and neurotoxicity by rifampicin. Its possible function as a hydroxyl radical scavenger
    • Tomiyama T, Shoji A, Kataoka K, Suwa Y, Asano S, Kaneko H, Endo N: Inhibition of amyloid β protein aggregation and neurotoxicity by rifampicin. Its possible function as a hydroxyl radical scavenger. J Biol Chem (1996) 271(12):6839-6844.
    • (1996) J Biol Chem , vol.271 , Issue.12 , pp. 6839-6844
    • Tomiyama, T.1    Shoji, A.2    Kataoka, K.3    Suwa, Y.4    Asano, S.5    Kaneko, H.6    Endo, N.7
  • 27
    • 18544389064 scopus 로고    scopus 로고
    • Parker MH, Chen R, Conway KA, Lee DH, Luo C, Boyd RE, Nortey SO, Ross TM, Scott MK, Reitz AB: Synthesis of (-)-5,8-dihydroxy-3R-methyl-2R- (dipropylamino)-1,2,3,4-tetrahydronaphthalene: An inhibitor of β-amyloid(1-42) aggregation. Bioorg Med Chem (2002) 10(11):3565-3569.
    • Parker MH, Chen R, Conway KA, Lee DH, Luo C, Boyd RE, Nortey SO, Ross TM, Scott MK, Reitz AB: Synthesis of (-)-5,8-dihydroxy-3R-methyl-2R- (dipropylamino)-1,2,3,4-tetrahydronaphthalene: An inhibitor of β-amyloid(1-42) aggregation. Bioorg Med Chem (2002) 10(11):3565-3569.
  • 28
    • 0037084186 scopus 로고    scopus 로고
    • Type IV collagen prevents amyloid β-protein fibril formation
    • Kiuchi Y, Isobe Y, Fukushima K: Type IV collagen prevents amyloid β-protein fibril formation. Life Sci (2002) 70(13):1555- 1564.
    • (2002) Life Sci , vol.70 , Issue.13 , pp. 1555-1564
    • Kiuchi, Y.1    Isobe, Y.2    Fukushima, K.3
  • 30
    • 0033569444 scopus 로고    scopus 로고
    • Common structural features determine the effectiveness of carvedilol, daunomycin and rolitetracycline as inhibitors of Alzheimer β-amyloid fibril formation
    • Howlett DR, George AR, Owen DE, Ward RV, Markwell RE: Common structural features determine the effectiveness of carvedilol, daunomycin and rolitetracycline as inhibitors of Alzheimer β-amyloid fibril formation. Biochem J (1999) 343(Pt 2):419-423.
    • (1999) Biochem J , vol.343 , Issue.PART 2 , pp. 419-423
    • Howlett, D.R.1    George, A.R.2    Owen, D.E.3    Ward, R.V.4    Markwell, R.E.5
  • 31
    • 0033572813 scopus 로고    scopus 로고
    • Interactions of Alzheimer amyloid-β peptides with glycosaminoglycans effects on fibril nucleation and growth
    • McLaurin J, Franklin T, Zhang X, Deng J, Fraser PE: Interactions of Alzheimer amyloid-β peptides with glycosaminoglycans effects on fibril nucleation and growth. Eur J Biochem (1999) 266(3):1101-1110.
    • (1999) Eur J Biochem , vol.266 , Issue.3 , pp. 1101-1110
    • McLaurin, J.1    Franklin, T.2    Zhang, X.3    Deng, J.4    Fraser, P.E.5
  • 32
    • 0037418703 scopus 로고    scopus 로고
    • Fullerene inhibits β-amyloid peptide aggregation
    • Kim JE, Lee M: Fullerene inhibits β-amyloid peptide aggregation. Biochem Biophys Res Commun (2003) 303(2):576-579.
    • (2003) Biochem Biophys Res Commun , vol.303 , Issue.2 , pp. 576-579
    • Kim, J.E.1    Lee, M.2
  • 33
    • 0037044835 scopus 로고    scopus 로고
    • New class of inhibitors of amyloid-β fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease
    • Lashuel HA, Hartley DM, Balakhaneh D, Aggarwal A, Teichberg S, Callaway DJ: New class of inhibitors of amyloid-β fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease. J Biol Chem (2002) 277(45):42881-42890.
    • (2002) J Biol Chem , vol.277 , Issue.45 , pp. 42881-42890
    • Lashuel, H.A.1    Hartley, D.M.2    Balakhaneh, D.3    Aggarwal, A.4    Teichberg, S.5    Callaway, D.J.6
  • 36
    • 1242316922 scopus 로고    scopus 로고
    • Aβ aggregation inhibitors. Part 1: Synthesis and biological activity of phenylazo benzene-sulfonamides
    • Lin SJ, Shiao YJ, Chi CW, Yang LM: Aβ aggregation inhibitors. Part 1: Synthesis and biological activity of phenylazo benzene-sulfonamides. Bioorg Med Chem Lett (2004) 14(5):1173-1176.
    • (2004) Bioorg Med Chem Lett , vol.14 , Issue.5 , pp. 1173-1176
    • Lin, S.J.1    Shiao, Y.J.2    Chi, C.W.3    Yang, L.M.4
  • 37
    • 25144471718 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation of β-amyloid peptides via the amphiphilic surfactants
    • Wang SS, Chen YT, Chou SW: Inhibition of amyloid fibril formation of β-amyloid peptides via the amphiphilic surfactants. Biochim Biophys Acta (2005) 1741(3):307-331.
    • (2005) Biochim Biophys Acta , vol.1741 , Issue.3 , pp. 307-331
    • Wang, S.S.1    Chen, Y.T.2    Chou, S.W.3
  • 38
    • 20044370990 scopus 로고    scopus 로고
    • Yang F, Lim GP, Begum AN, Ubeda OJ, Simmons MR, Ambegaokar SS, Chen PP, Kayed R, Glabe CG, Frautschy SA, Cole GM: Curcumin inhibits formation of amyloid β oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J Biol Chem (2005) 280(7):5892-5901. • The spice curcumin is an effective inhibitor of Aβ toxicity in vitro and in vivo.
    • Yang F, Lim GP, Begum AN, Ubeda OJ, Simmons MR, Ambegaokar SS, Chen PP, Kayed R, Glabe CG, Frautschy SA, Cole GM: Curcumin inhibits formation of amyloid β oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J Biol Chem (2005) 280(7):5892-5901. • The spice curcumin is an effective inhibitor of Aβ toxicity in vitro and in vivo.
  • 39
    • 9144235581 scopus 로고    scopus 로고
    • Rzepecki P, Nagel-Steger L, Feuerstein S, Linne U, Molt O, Zadmard R, Aschermann K, Wehner M, Schrader T, Riesner D: Prevention of Alzheimer's disease-associated Aβ aggregation by rationally designed nonpeptidic β-sheet ligands. J Biol Chem (2004) 279(46): 47497-47505. • Inhibitors can be designed to maintain the hydrogen-bonding pattern present in β-sheets.
    • Rzepecki P, Nagel-Steger L, Feuerstein S, Linne U, Molt O, Zadmard R, Aschermann K, Wehner M, Schrader T, Riesner D: Prevention of Alzheimer's disease-associated Aβ aggregation by rationally designed nonpeptidic β-sheet ligands. J Biol Chem (2004) 279(46): 47497-47505. • Inhibitors can be designed to maintain the hydrogen-bonding pattern present in β-sheets.
  • 40
    • 0034674785 scopus 로고    scopus 로고
    • Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid β peptide and inhibit Aβ induced toxicity
    • McLaurin J, Golomb R, Jurewicz A, Antel JP, Fraser PE: Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid β peptide and inhibit Aβ induced toxicity. J Biol Chem (2000) 275(24):18495-18502.
    • (2000) J Biol Chem , vol.275 , Issue.24 , pp. 18495-18502
    • McLaurin, J.1    Golomb, R.2    Jurewicz, A.3    Antel, J.P.4    Fraser, P.E.5
  • 42
    • 33745096194 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism
    • Porat Y, Abramowitz A, Gazit E: Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism. Chem Biol Drug Des (2006) 67(1):27-37.
    • (2006) Chem Biol Drug Des , vol.67 , Issue.1 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 43
    • 33845388059 scopus 로고    scopus 로고
    • A phase II study targeting amyloid-β with 3APS in mild-to-moderate Alzheimer disease
    • Aisen PS, Saumier D, Briand R, Laurin J, Gervais F, Tremblay P, Garceau D: A phase II study targeting amyloid-β with 3APS in mild-to-moderate Alzheimer disease. Neurology (2006) 67(10):1757-1763.
    • (2006) Neurology , vol.67 , Issue.10 , pp. 1757-1763
    • Aisen, P.S.1    Saumier, D.2    Briand, R.3    Laurin, J.4    Gervais, F.5    Tremblay, P.6    Garceau, D.7
  • 45
    • 0035049210 scopus 로고    scopus 로고
    • Salvianolic acid B inhibits fibril formation and neurotoxicity of amyloid β-protein in vitro
    • Tang NK, Zhang JT: Salvianolic acid B inhibits fibril formation and neurotoxicity of amyloid β-protein in vitro. Acta Pharmacol Sin (2001) 22(4):380-384.
    • (2001) Acta Pharmacol Sin , vol.22 , Issue.4 , pp. 380-384
    • Tang, N.K.1    Zhang, J.T.2
  • 47
    • 7444221875 scopus 로고    scopus 로고
    • Harnessing chaperones to generate small-molecule inhibitors of amyloid β aggregation
    • Gestwicki JE, Crabtree GR, Graef IA: Harnessing chaperones to generate small-molecule inhibitors of amyloid β aggregation. Science (2004) 306(5697):865-869.
    • (2004) Science , vol.306 , Issue.5697 , pp. 865-869
    • Gestwicki, J.E.1    Crabtree, G.R.2    Graef, I.A.3
  • 48
    • 0029994633 scopus 로고    scopus 로고
    • Tjernberg LO, Näslund J, Lindqvist F, Johansson J, Karlström AR, Thyberg J, Terenius L, Nordstedt C: Arrest of β-amyloid fibril formation by a pentapeptide ligand. J Biol Chem (1996) 271(15): 8545-8548. • Identification of KLVFF as the key amyloidogenic domain of Aβ - the core of most peptide inhibitors of Aβ aggregation.
    • Tjernberg LO, Näslund J, Lindqvist F, Johansson J, Karlström AR, Thyberg J, Terenius L, Nordstedt C: Arrest of β-amyloid fibril formation by a pentapeptide ligand. J Biol Chem (1996) 271(15): 8545-8548. • Identification of KLVFF as the key amyloidogenic domain of Aβ - the core of most peptide inhibitors of Aβ aggregation.
  • 50
    • 2642557773 scopus 로고    scopus 로고
    • Eight-residue Aβ peptides inhibit the aggregation and enzymatic activity of Aβ42
    • Matsunaga Y, Fujii A, Awasthi A, Yokotani J, Takakura T, Yamada T: Eight-residue Aβ peptides inhibit the aggregation and enzymatic activity of Aβ42. Regul Pept (2004) 120(1-3):227-236.
    • (2004) Regul Pept , vol.120 , Issue.1-3 , pp. 227-236
    • Matsunaga, Y.1    Fujii, A.2    Awasthi, A.3    Yokotani, J.4    Takakura, T.5    Yamada, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.