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Volumn 9, Issue 1, 2013, Pages 67-74

Trisubstituted Phenolic compounds as inhibitors of Acetylcholinesterase and Amyloid beta aggregate formation

Author keywords

Acetylcholinesterase; Aggregation; Alzheimer's disease; Amyloid beta; Dual inhibitors; Phenol

Indexed keywords

ACETYLCHOLINESTERASE; AMYLOID BETA PROTEIN; ELLAGIC ACID; GALLIC ACID; JUGLANS REGIA EXTRACT; PHENOL DERIVATIVE; PLANT EXTRACT; UNCLASSIFIED DRUG;

EID: 84877324380     PISSN: 15734080     EISSN: 18756662     Source Type: Journal    
DOI: 10.2174/1573408011309010009     Document Type: Article
Times cited : (9)

References (32)
  • 1
    • 79959370222 scopus 로고    scopus 로고
    • Disease-modifying treatments for Alzheimer's disease
    • Galimberti, D.; Scarpini, E. Disease-modifying treatments for Alzheimer's disease. Ther. Adv. Neurol. Disord., 2011, 4, 203-216.
    • (2011) Ther. Adv. Neurol. Disord , vol.4 , pp. 203-216
    • Galimberti, D.1    Scarpini, E.2
  • 2
    • 78651380121 scopus 로고    scopus 로고
    • Alzeheimer disease: Update on basic mechanisms
    • Xiaoning, B. Alzeheimer disease: update on basic mechanisms. J. Am. Osteopath. Assoc, 2010, 110, S3-S9.
    • (2010) J. Am. Osteopath. Assoc , vol.110
    • Xiaoning, B.1
  • 3
    • 0032080309 scopus 로고    scopus 로고
    • Stable complexes involving acetylcholinesterase and amyloid-p peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils
    • Alvarez, A.; Alarcon, R.; Opazo, C; Campos, E.O.; Munoz, F.J.; Calderon, F.H.; Dajas, F.; Gentry, M.K.; Doctor, B.P.; De Mello, F.G.; Inestrosa, N.C. Stable complexes involving acetylcholinesterase and amyloid-p peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils. J. Neurosci., 1998, 18, 3213-3223.
    • (1998) J. Neurosci , vol.18 , pp. 3213-3223
    • Alvarez, A.1    Alarcon, R.2    Opazo, C.3    Campos, E.O.4    Munoz, F.J.5    Calderon, F.H.6    Dajas, F.7    Gentry, M.K.8    Doctor, B.P.9    de Mello, F.G.10    Inestrosa, N.C.11
  • 4
    • 68149162581 scopus 로고    scopus 로고
    • Soluble fibrillar oligomer levels are elevated in Alzheimer disease brain and correlate with cognitive dysfunction
    • Tornic, J.L.; Pensalfini, A.; Head, E.; Glabe, D.G. Soluble fibrillar oligomer levels are elevated in Alzheimer disease brain and correlate with cognitive dysfunction. Neurobiol. Dis., 2009, 35, 352-358.
    • (2009) Neurobiol. Dis , vol.35 , pp. 352-358
    • Tornic, J.L.1    Pensalfini, A.2    Head, E.3    Glabe, D.G.4
  • 5
    • 0035949487 scopus 로고    scopus 로고
    • Presenilin, notch and the genesis and treatment of Alzheimer's disease
    • Selkoe, D.J. Presenilin, notch and the genesis and treatment of Alzheimer's disease. PNAS, 2001, 98, 11039-11041.
    • (2001) PNAS , vol.98 , pp. 11039-11041
    • Selkoe, D.J.1
  • 6
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid p-peptide
    • Haass, C; Selkoe, D.J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid p-peptide. Nat. Rev. Mol. Cell Biol, 2007, 8, 101-112.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 7
    • 0031587286 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes the aggregation of amyloid-p-peptide fragments by forming a complex with the growing fibrils
    • Alvarez, A.; Opazo, C; Alarcon, R.; Garrido, J.; Inestrosa, N.C. Acetylcholinesterase promotes the aggregation of amyloid-p-peptide fragments by forming a complex with the growing fibrils. J. Mol. Biol, 1997, 272, 348-361.
    • (1997) J. Mol. Biol , vol.272 , pp. 348-361
    • Alvarez, A.1    Opazo, C.2    Alarcon, R.3    Garrido, J.4    Inestrosa, N.C.5
  • 8
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-p-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme
    • Inestrosa, N.C; Alvarez, A; Perez, C.A; Moreno, R.D.; Vicente, M.; Linker, C; Casanueva, O.I.; Soto, C; Garrido, J. Acetylcholinesterase accelerates assembly of amyloid-p-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron, 1996, 16, 881-891.
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Perez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6    Casanueva, O.I.7    Soto, C.8    Garrido, J.9
  • 9
    • 0033583819 scopus 로고    scopus 로고
    • The Adhesion function on acetylcholinesterase is located at the peripheral anionic site
    • Johnson, G.; Moore, S.W. The Adhesion function on acetylcholinesterase is located at the peripheral anionic site. Biochem. Biophys. Res. Commun., 1999, 258, 758-762.
    • (1999) Biochem. Biophys. Res. Commun , vol.258 , pp. 758-762
    • Johnson, G.1    Moore, S.W.2
  • 11
    • 78651472058 scopus 로고    scopus 로고
    • Design, synthesis and evaluation of novel tacrine-multialkoxybenzene hybrids as dual inhibitors for cholinesterases and amyloid beta aggregation
    • Luo, W.; Li, Y-P.; He, Y.; Huang, S-L.; Tan, J-H.; Ou, T-M.; Li, D.; Gu, L-Q.; Huang, Z-S. Design, synthesis and evaluation of novel tacrine-multialkoxybenzene hybrids as dual inhibitors for cholinesterases and amyloid beta aggregation. Bioorg. Med. Chem., 2011, 19, 763-770.
    • (2011) Bioorg. Med. Chem , vol.19 , pp. 763-770
    • Luo, W.1    Li, Y.-P.2    He, Y.3    Huang, S.-L.4    Tan, J.-H.5    Ou, T.-M.6    Li, D.7    Gu, L.-Q.8    Huang, Z.-S.9
  • 12
    • 75149165246 scopus 로고    scopus 로고
    • Synthesis, biological evaluation, and molecular modeling of berberine derivatives as potent acetylcholinesterase inhibitors
    • Huang, L.; Shi, A.; He, F.; Li, X. Synthesis, biological evaluation, and molecular modeling of berberine derivatives as potent acetylcholinesterase inhibitors. Bioorg. Med. Chem., 2010, 18, 1244-1251.
    • (2010) Bioorg. Med. Chem , vol.18 , pp. 1244-1251
    • Huang, L.1    Shi, A.2    He, F.3    Li, X.4
  • 13
    • 33644811612 scopus 로고
    • A new and rapid colorimetric determination of acetylcholinesterase activity
    • Ellman, G.L.; Courtney, K.D.; Andres, V.; Featherstone, R.M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol, 1961, 7, 88-95.
    • (1961) Biochem. Pharmacol , vol.7 , pp. 88-95
    • Ellman, G.L.1    Courtney, K.D.2    Andres, V.3    Featherstone, R.M.4
  • 14
    • 24144478984 scopus 로고    scopus 로고
    • Walnut extract inhibits the fibrillization of amyloid beta-protein, and also defibrillizes its preformed fibrils
    • Chauhan, N.; Wang, K.C.; Wegiel, J.; Malik, M.N. Walnut extract inhibits the fibrillization of amyloid beta-protein, and also defibrillizes its preformed fibrils. Curr. Alzheimer Res., 2004, 1, 183-188.
    • (2004) Curr. Alzheimer Res , vol.1 , pp. 183-188
    • Chauhan, N.1    Wang, K.C.2    Wegiel, J.3    Malik, M.N.4
  • 15
    • 0032899322 scopus 로고    scopus 로고
    • Quantifying amyloid p-peptide aggregation using the congo red-Ap spectrophotometric assay
    • Klunk, W.E.; Jacob, R.F.; Mason, R.P. Quantifying amyloid p-peptide aggregation using the congo red-Ap spectrophotometric assay. Anal. Biochem., 1999, 266, 66-76.
    • (1999) Anal. Biochem , vol.266 , pp. 66-76
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 16
    • 0024352110 scopus 로고
    • Quantitative evaluation of CR binding to amyloid-like proteins with a beta pleated sheet conformation
    • Klunk, W.E.; Pettegrew, J.W.; Abraham, D.J. Quantitative evaluation of CR binding to amyloid-like proteins with a beta pleated sheet conformation. J. Histochem. Cytochem., 1989, 37, 1273-1281.
    • (1989) J. Histochem. Cytochem , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 17
    • 77951867859 scopus 로고    scopus 로고
    • Oxidative stress and Alzheimer's disease: Dietary polyphenols as potential therapeutic agents. Expert
    • Darvesh, A.S.; Carroll, R.T.; Bishayee, A.; Geldenhuys, W.J.; Van Der Schyf, C.J. Oxidative stress and Alzheimer's disease: dietary polyphenols as potential therapeutic agents. Expert Rev. Neurother., 2010, 10, 729-745.
    • (2010) Rev. Neurother , vol.10 , pp. 729-745
    • Darvesh, A.S.1    Carroll, R.T.2    Bishayee, A.3    Geldenhuys, W.J.4    Van Der Schyf, C.J.5
  • 18
    • 56349157854 scopus 로고    scopus 로고
    • Benefits from dietary polyphenols for brain aging and Alzheimer's disease
    • Rossi, L.; Mazzitelli, S.; Arciello, M.; Capo, C.R.; Rotilio, G. Benefits from dietary polyphenols for brain aging and Alzheimer's disease. Neurochem. Res., 2008, 33, 2390-400.
    • (2008) Neurochem. Res , vol.33 , pp. 2390-2400
    • Rossi, L.1    Mazzitelli, S.2    Arciello, M.3    Capo, C.R.4    Rotilio, G.5
  • 19
    • 47849120398 scopus 로고    scopus 로고
    • Challenges for research on polyphenols from foods in Alzheimer's disease: Bioavailability, metabolism, and cellular and molecular mechanisms
    • Singh, M.; Arseneault, M.; Sanderson, T.; Murthy, V.; Ramassamy, C. Challenges for research on polyphenols from foods in Alzheimer's disease: bioavailability, metabolism, and cellular and molecular mechanisms. J. Agric. Food Chem., 2008, 56, 4855-4873.
    • (2008) J. Agric. Food Chem , vol.56 , pp. 4855-4873
    • Singh, M.1    Arseneault, M.2    Sanderson, T.3    Murthy, V.4    Ramassamy, C.5
  • 21
    • 48849104834 scopus 로고    scopus 로고
    • Molecules that target beta-amyloid
    • Stains, C.I.; Mondal, K.; Ghosh, I. Molecules that target beta-amyloid. Chem. Med. Chem., 2007, 2, 1674-1692.
    • (2007) Chem. Med. Chem , vol.2 , pp. 1674-1692
    • Stains, C.I.1    Mondal, K.2    Ghosh, I.3
  • 22
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman, J.L.; Harel, M.; Frolow, F.; Oefner, C.; Godman, A.; Toker, L.; Silman, I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science, 1991, 253, 872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Godman, A.5    Toker, L.6    Silman, I.7
  • 24
    • 0000694113 scopus 로고
    • Acetylcholinesterase: Structure and use as a model for specific cation-protein interactions
    • Sussman, J.L.; Silman, I. Acetylcholinesterase: structure and use as a model for specific cation-protein interactions. Curr. Opin. Struct. Biol., 1992, 2, 721-729.
    • (1992) Curr. Opin. Struct. Biol , vol.2 , pp. 721-729
    • Sussman, J.L.1    Silman, I.2
  • 26
    • 33644867844 scopus 로고    scopus 로고
    • The peripheral anionic site of acetylcholinesterase: Structure, functions and potential role in rational drug design
    • Johnson, G.; Moore, S.W. The peripheral anionic site of acetylcholinesterase: structure, functions and potential role in rational drug design. Curr. Pharm. Des., 2006, 12, 217-225.
    • (2006) Curr. Pharm. Des , vol.12 , pp. 217-225
    • Johnson, G.1    Moore, S.W.2
  • 28
    • 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, 27-37.
    • (2006) Chem. Biol. Drug Des , vol.67 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 30
    • 79955806884 scopus 로고    scopus 로고
    • Mutations That Replace Aromatic Side Chains Promote Aggregation of the Alzheimer's Aβ Peptide
    • Armstrong, A.H.; Chen, J.; McKoy, A.F.; Hecht, M.H. Mutations That Replace Aromatic Side Chains Promote Aggregation of the Alzheimer's Aβ Peptide. Biochemistry, 2011, 50, 4058-4067.
    • (2011) Biochemistry , vol.50 , pp. 4058-4067
    • Armstrong, A.H.1    Chen, J.2    McKoy, A.F.3    Hecht, M.H.4
  • 31
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
    • Necula, M.; Kayed, R.; Milton, S.; Glabe, C.G. Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct. J. Biol. Chem., 2007, 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
  • 32
    • 0000140355 scopus 로고    scopus 로고
    • Non-equilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands
    • Szegletes, T.; Mallender, W.D.; Rosenberry, T.L. Non-equilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands. Biochemistry, 1998, 37, 4206-4216.
    • (1998) Biochemistry , vol.37 , pp. 4206-4216
    • Szegletes, T.1    Mallender, W.D.2    Rosenberry, T.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.