메뉴 건너뛰기




Volumn 12, Issue 1, 2011, Pages 694-724

In silico theoretical molecular modeling for Alzheimer's disease: The nicotine-curcumin paradigm in neuroprotection and neurotherapy

Author keywords

Alzheimer's disease; Amyloid ; Artificial neural networks; Central composite design; Constraint optimization; Curcumin; Docking; Isobolographic analysis; Ligand protein complexes; Molecular mechanics; Nicotine; Protein; Synergism

Indexed keywords

2,9 DIMETHYL 1,10 PHENANTHROLINE; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; APIGENIN; BENZOPHENONE DERIVATIVE; CONGO RED; CURCUMIN; DIHYDROXYBENZOPHENONE; GLYCOSYLATED NORNICOTINE; HEXAMETHYLPYRIDINIUM; INDOMETACIN; MOLECULAR SCAFFOLD; NORNICOTINE; POLYSTYRENESULFONIC ACID; PYRIDINIUM DERIVATIVE; THIOFLAVINE; UNCLASSIFIED DRUG; NEUROPROTECTIVE AGENT; NICOTINE;

EID: 79251636605     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms12010694     Document Type: Article
Times cited : (50)

References (42)
  • 1
    • 56249097900 scopus 로고    scopus 로고
    • The plaque plan
    • Abbott, A. The plaque plan. Nature 2008, 456, 161-164.
    • (2008) Nature , vol.456 , pp. 161-164
    • Abbott, A.1
  • 3
    • 33646473959 scopus 로고    scopus 로고
    • Therapeutic potential of controlled drug delivery systems in neurodegenerative diseases
    • Popovic, N.; Brundin, P. Therapeutic potential of controlled drug delivery systems in neurodegenerative diseases. Int. J. Pharm. 2006, 314, 120-126.
    • (2006) Int. J. Pharm , vol.314 , pp. 120-126
    • Popovic, N.1    Brundin, P.2
  • 4
    • 68249158658 scopus 로고    scopus 로고
    • Neurodegenerative disorders and nanoformulated drug development: Executive summary
    • Nowacek, A.; Kosloski, L.M.; Gendelman, H.E. Neurodegenerative disorders and nanoformulated drug development: Executive summary. Nanomedicine 2009, 4, 541-555.
    • (2009) Nanomedicine , vol.4 , pp. 541-555
    • Nowacek, A.1    Kosloski, L.M.2    Gendelman, H.E.3
  • 5
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe, D.J. The molecular pathology of Alzheimer's disease. Neuron 1991, 6, 487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 6
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy, J. Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. 1997, 20, 154-159.
    • (1997) Trends Neurosci , vol.20 , pp. 154-159
    • Hardy, J.1
  • 7
    • 70350075694 scopus 로고    scopus 로고
    • Alzheimer's disease
    • Mucke, L. Alzheimer's disease. Nature 2009, 461, 895-897.
    • (2009) Nature , vol.461 , pp. 895-897
    • Mucke, L.1
  • 8
    • 77956402632 scopus 로고    scopus 로고
    • Curcumin and Alzheimer's Disease
    • doi:10.1111/j.1755-5949.2010.00147.x
    • Hamaguchi, T.; Ono, K.; Yamada, M. Curcumin and Alzheimer's Disease. CNS Neurosci. Therap. 2010, doi:10.1111/j.1755-5949.2010.00147.x.
    • (2010) CNS Neurosci. Therap
    • Hamaguchi, T.1    Ono, K.2    Yamada, M.3
  • 10
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • Haass, C.; Selkoe, D.J. Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-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
  • 11
    • 33746649088 scopus 로고    scopus 로고
    • Anti-amyloidogenic therapies: Strategies for prevention and treatment of Alzheimer's disease
    • Hamaguchi, T.; Ono, K.; Yamada, M. Anti-amyloidogenic therapies: Strategies for prevention and treatment of Alzheimer's disease. Cell Mol. Life Sci. 2006, 63, 1538-1552.
    • (2006) Cell Mol. Life Sci , vol.63 , pp. 1538-1552
    • Hamaguchi, T.1    Ono, K.2    Yamada, M.3
  • 12
    • 0037478709 scopus 로고    scopus 로고
    • Glycation of the amyloid β-protein by a nicotine metabolite: A fortuitous chemical dynamic between smoking and Alzheimer's disease
    • Dickerson, T.J.; Janda, K.D. Glycation of the amyloid β-protein by a nicotine metabolite: A fortuitous chemical dynamic between smoking and Alzheimer's disease. Proc. Natl. Acad. Sci. USA 2003, 100, 8182-8187.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8182-8187
    • Dickerson, T.J.1    Janda, K.D.2
  • 13
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin has potent anti-amyloidogenic effects for Alzheimer's beta-amyloid fibrils in vitro
    • Ono, K.; Hasegawa, K.; Naiki, H.; Yamada, M. Curcumin has potent anti-amyloidogenic effects for Alzheimer's beta-amyloid fibrils in vitro. J. Neurosci. Res. 2004, 75, 742-750.
    • (2004) J. Neurosci. Res , vol.75 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 14
    • 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. The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 2002, 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 15
    • 15944426127 scopus 로고    scopus 로고
    • Amyloid accumulation and pathogenesis of Alzheimer's
    • Glabe, C.C. Amyloid accumulation and pathogenesis of Alzheimer's. Subcell Biochem. 2005, 38, 167-177.
    • (2005) Subcell Biochem , vol.38 , pp. 167-177
    • Glabe, C.C.1
  • 16
    • 0026619343 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid beta A4 peptides of Alzheimer's disease
    • Hilbich, C.; Kisters-Woike, B.; Reed, J.; Masters, C.L.; Beyreuther, K. Aggregation and secondary structure of synthetic amyloid beta A4 peptides of Alzheimer's disease. J. Mol. Biol. 1992, 228, 460-473.
    • (1992) J. Mol. Biol , vol.228 , pp. 460-473
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 19
    • 0026101636 scopus 로고
    • Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides
    • Hilbich, C.; Kisters-Woike, B.; Reed, J.; Masters, C.L.; Beyreuther, K. Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides. J. Mol. Biol. 1991, 218, 149-163.
    • (1991) J. Mol. Biol , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 20
    • 14844303721 scopus 로고    scopus 로고
    • Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins
    • Taniguchi, S.; Suzuki, N.; Masuda, M.; Hisanaga, S.; Iwatsubo, T.; Goedert, M.; Hasegawa, M. Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins. J. Biol. Chem. 2005, 280, 7614-7623.
    • (2005) J. Biol. Chem , vol.280 , pp. 7614-7623
    • Taniguchi, S.1    Suzuki, N.2    Masuda, M.3    Hisanaga, S.4    Iwatsubo, T.5    Goedert, M.6    Hasegawa, M.7
  • 22
    • 17144395539 scopus 로고    scopus 로고
    • Triggers of full-length tau aggregation: A role for partially folded intermediates
    • Chirita, C.N.; Congdon, E.E.; Yin, H.; Kuret, J. Triggers of full-length tau aggregation: A role for partially folded intermediates. Biochemistry 2005, 44, 5862-5872.
    • (2005) Biochemistry , vol.44 , pp. 5862-5872
    • Chirita, C.N.1    Congdon, E.E.2    Yin, H.3    Kuret, J.4
  • 23
    • 0031821321 scopus 로고    scopus 로고
    • Indomethacin reverses the microglial response to amyloid beta-protein
    • Netland, E.E.; Newton, J.L.; Majocha, R.E.; Tate, B.A. Indomethacin reverses the microglial response to amyloid beta-protein. Neurobiol. Aging 1998, 19, 201-204.
    • (1998) Neurobiol. Aging , vol.19 , pp. 201-204
    • Netland, E.E.1    Newton, J.L.2    Majocha, R.E.3    Tate, B.A.4
  • 24
    • 14844363573 scopus 로고    scopus 로고
    • Temperature dependence of the nucleation constant rate in beta amyloid fibrillogenesis
    • Sabate, R.; Gallardo, M.; Estelrich, J. Temperature dependence of the nucleation constant rate in beta amyloid fibrillogenesis. Int. J. Biol. Macromol. 2005, 35, 9-13.
    • (2005) Int. J. Biol. Macromol , vol.35 , pp. 9-13
    • Sabate, R.1    Gallardo, M.2    Estelrich, J.3
  • 25
    • 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. Small molecule inhibitors of aggregation indicate that amyloid beta 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
  • 26
    • 77951681963 scopus 로고    scopus 로고
    • Dual effect of amino modified polystyrene nanoparticles on amyloid β protein fibrillation
    • Cabaleiro-Lago, C.; Quinlan-Pluck, F.; Lynch, I.; Dawson, K.A.; Linse, S. Dual effect of amino modified polystyrene nanoparticles on amyloid β protein fibrillation. ACS Chem. Neurosci. 2010, 1, 279-287.
    • (2010) ACS Chem. Neurosci , vol.1 , pp. 279-287
    • Cabaleiro-Lago, C.1    Quinlan-Pluck, F.2    Lynch, I.3    Dawson, K.A.4    Linse, S.5
  • 27
    • 0008878905 scopus 로고    scopus 로고
    • Molecular mechanics calculations on protein-ligand complexes
    • Weber, I.T.; Harrison, R.W. Molecular mechanics calculations on protein-ligand complexes. Persp. Drug Disc. Des. 1998, 9-11, 115-127.
    • (1998) Persp. Drug Disc. Des , vol.9 , pp. 115-127
    • Weber, I.T.1    Harrison, R.W.2
  • 28
    • 0041348725 scopus 로고    scopus 로고
    • Optimization of an effervescent tablet formulation containing spray dried l-leucine and polyethylene glycol 6000 as lubricants using a central composite design
    • Rotthäuser, B.; Krausb, G.; Schmidt, P.C. Optimization of an effervescent tablet formulation containing spray dried l-leucine and polyethylene glycol 6000 as lubricants using a central composite design. Eur. J. Pharm. Biopharm. 1998, 46, 85-94.
    • (1998) Eur. J. Pharm. Biopharm , vol.46 , pp. 85-94
    • Rotthäuser, B.1    Krausb, G.2    Schmidt, P.C.3
  • 29
    • 21444434772 scopus 로고    scopus 로고
    • Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology
    • He, G.; Xuan, G.; Ruan, H.; Chen, Q.; Xu, Y. Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology. J. Zhejiang Univ. SCI. 2005, 6B, 508-513.
    • (2005) J. Zhejiang Univ. SCI , vol.6 B , pp. 508-513
    • He, G.1    Xuan, G.2    Ruan, H.3    Chen, Q.4    Xu, Y.5
  • 30
    • 58349090022 scopus 로고    scopus 로고
    • Central composite design-based analysis of specific leaf area and related agronomic factors in cultivars of rapeseed (Brassica napus L.)
    • Liu, T.; Zhang, C.; Yang, G; Wua, J.; Xie, G.; Zeng, H.; Yin, C.; Liu, T. Central composite design-based analysis of specific leaf area and related agronomic factors in cultivars of rapeseed (Brassica napus L.). Field Crop Res. 2009, 111, 92-96.
    • (2009) Field Crop Res , vol.111 , pp. 92-96
    • Liu, T.1    Zhang, C.2    Yang, G.3    Wua, J.4    Xie, G.5    Zeng, H.6    Yin, C.7    Liu, T.8
  • 31
    • 34250614668 scopus 로고    scopus 로고
    • Optimization of copper cementation process by iron using central composite design experiments
    • Djoudi, W.; Aissani-Benissad, F.; Bourouina-Bacha, S. Optimization of copper cementation process by iron using central composite design experiments. Chem. Engl. J. 2007, 133, 1-6.
    • (2007) Chem. Engl. J , vol.133 , pp. 1-6
    • Djoudi, W.1    Aissani-Benissad, F.2    Bourouina-Bacha, S.3
  • 33
    • 0028013301 scopus 로고
    • Topography of a binding site for small amnestic peptides deduced from structure-activity studies: Relation to amnestic effect of amyloid beta protein
    • Flood, J.F.; Roberts, E.; Sherman, M.A.; Kaplan, B.E.; Morley, J.E. Topography of a binding site for small amnestic peptides deduced from structure-activity studies: Relation to amnestic effect of amyloid beta protein. Proc. Natl. Acad. Sci. USA 1994, 91, 380-384.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 380-384
    • Flood, J.F.1    Roberts, E.2    Sherman, M.A.3    Kaplan, B.E.4    Morley, J.E.5
  • 34
    • 77955084717 scopus 로고    scopus 로고
    • Why pleiotropic interventions are needed for alzheimer's disease?
    • Frautschy, S.A.; Cole, G.M. Why pleiotropic interventions are needed for alzheimer's disease? Mol. Neurobiol. 2010, 41, 392-409.
    • (2010) Mol. Neurobiol , vol.41 , pp. 392-409
    • Frautschy, S.A.1    Cole, G.M.2
  • 35
    • 84856114590 scopus 로고    scopus 로고
    • RCSB Protein Data Bank, accessed on 18 April 2010
    • RCSB Protein Data Bank. Available online: www.pdb.org (accessed on 18 April 2010).
  • 36
    • 84856116114 scopus 로고    scopus 로고
    • Chemical Entities of Biological Interest (ChEBI), accessed on 22 April 2010
    • Chemical Entities of Biological Interest (ChEBI). Available online: www.ebi.ac.uk/chebi (accessed on 22 April 2010).
  • 37
    • 84856114591 scopus 로고    scopus 로고
    • The TDR Targets Database v4, accessed on 22 April 2010
    • The TDR Targets Database v4. Available online: www.tdrtargets.org (accessed on 22 April 2010)
  • 38
    • 84856116115 scopus 로고    scopus 로고
    • PubChem structure search, accessed on 22 April 2010
    • PubChem structure search. Available online: www.pubchem.ncbi.nlm.nih.gov (accessed on 22 April 2010).
  • 39
    • 0037424611 scopus 로고    scopus 로고
    • Artificial neural networks and genetic algorithms in QSAR
    • Niculescu, S.P. Artificial neural networks and genetic algorithms in QSAR. J. Mol. Struct. Theochem. 2003, 622, 71-83.
    • (2003) J. Mol. Struct. Theochem , vol.622 , pp. 71-83
    • Niculescu, S.P.1
  • 40
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics of organic liquids
    • Jorgensen, W.L.; Maxwell, D.S.; Tirado-Rives, J. Development and testing of the OPLS all-atom force field on conformational energetics of organic liquids. J. Am. Chem. Soc. 1996, 118, 11225-11236.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 41
    • 2342465506 scopus 로고    scopus 로고
    • Accurate calculations of ligand binding free energies
    • Hayes, M.J.; Stein, M.; Weiser, J. Accurate calculations of ligand binding free energies. J. Phys. Chem. 2004, 108, 3572-3580.
    • (2004) J. Phys. Chem , vol.108 , pp. 3572-3580
    • Hayes, M.J.1    Stein, M.2    Weiser, J.3
  • 42
    • 34250958584 scopus 로고
    • Effect of combinations: Mathematical basis of problem
    • Loewe, S.; Muchnik, H. Effect of combinations: Mathematical basis of problem. Arch. Exp. Pathol. Pharmacol. 1926, 114, 313-326.
    • (1926) Arch. Exp. Pathol. Pharmacol , vol.114 , pp. 313-326
    • Loewe, S.1    Muchnik, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.