메뉴 건너뛰기




Volumn 5, Issue 5, 2014, Pages 377-389

Acetylcholinesterase inhibitors with photoswitchable inhibition of β-amyloid aggregation

Author keywords

1,2 dithienylethene; Alzheimer's disease; beta amyloid aggregation; cholinesterase inhibitors; photochromism; tacrine

Indexed keywords

AMYLOID BETA PROTEIN; CARBON DIOXIDE; CARBOXYLIC ACID DERIVATIVE; CHOLINESTERASE INHIBITOR; ETHYLENEDIAMINE; TACRINE DERIVATIVE; PHOTOSENSITIZING AGENT; PROTEIN AGGREGATE;

EID: 84901246932     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn500016p     Document Type: Article
Times cited : (92)

References (64)
  • 2
    • 0037298750 scopus 로고    scopus 로고
    • β-Amyloid aggregation induced by human acetylcholinesterase: Inhibition studies
    • Bartolini, M., Bertucci, C., Cavrini, V., and Andrisano, V. (2003) β-Amyloid aggregation induced by human acetylcholinesterase: inhibition studies Biochem. Pharmacol. 65, 407-416
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 407-416
    • Bartolini, M.1    Bertucci, C.2    Cavrini, V.3    Andrisano, V.4
  • 3
    • 84866370563 scopus 로고    scopus 로고
    • Revisiting the role of acetylcholinesterase in Alzheimer's disease: Cross-talk with P-tau and β-amyloid
    • García-Allón, M.-S., Small, D. H., Avila, J., and Sáez-Valero, J. (2011) Revisiting the role of acetylcholinesterase in Alzheimer's disease: cross-talk with P-tau and β-amyloid Front. Mol. Neurosci. 4:22, 1-9
    • (2011) Front. Mol. Neurosci. , vol.422 , pp. 1-9
    • García-Allón, M.-S.1    Small, D.H.2    Avila, J.3    Sáez-Valero, J.4
  • 4
    • 84862879021 scopus 로고    scopus 로고
    • Interactions of AChE with Aβ aggregates in Alzheimer's brain; Therapeutic relevance of IDN 5706
    • Carvajal, F. J. and Inestrosa, N. C. (2011) Interactions of AChE with Aβ aggregates in Alzheimer's brain; therapeutic relevance of IDN 5706 Front. Mol. Neurosci. 4:19, 1-10
    • (2011) Front. Mol. Neurosci. , vol.419 , pp. 1-10
    • Carvajal, F.J.1    Inestrosa, N.C.2
  • 6
    • 12444257779 scopus 로고    scopus 로고
    • 3-(4-{[Benzyl(methyl)amino]methyl}phenyl)-6,7-dimethoxy-2 H -2-chromenone (AP2238) inhibits both acetylcholinesterase and acetylcholinesterase-induced β-amyloid aggregation: A dual function lead for Alzheimer's disease therapy
    • Piazzi, L., Rampa, A., Bisi, A., Gobbi, S., Belluti, F., Cavalli, A., Bartolini, M., Andrisano, V., Valenti, P., and Recanatini, M. (2003) 3-(4-{[Benzyl(methyl)amino]methyl}phenyl)-6,7-dimethoxy-2 H -2-chromenone (AP2238) inhibits both acetylcholinesterase and acetylcholinesterase-induced β-amyloid aggregation: A dual function lead for Alzheimer's disease therapy J. Med. Chem. 46, 2279-2282
    • (2003) J. Med. Chem. , vol.46 , pp. 2279-2282
    • Piazzi, L.1    Rampa, A.2    Bisi, A.3    Gobbi, S.4    Belluti, F.5    Cavalli, A.6    Bartolini, M.7    Andrisano, V.8    Valenti, P.9    Recanatini, M.10
  • 7
    • 84871094408 scopus 로고    scopus 로고
    • Recent advances in the multitarget-directed ligands approach for the treatment of Alzheimer's disease
    • León, R., Garcia, A. G., and Marco-Contelles, J. (2013) Recent advances in the multitarget-directed ligands approach for the treatment of Alzheimer's disease Med. Res. Rev. 33, 139-189
    • (2013) Med. Res. Rev. , vol.33 , pp. 139-189
    • León, R.1    Garcia, A.G.2    Marco-Contelles, J.3
  • 8
    • 42949132291 scopus 로고    scopus 로고
    • Design and synthesis of tacrine-ferulic acid hybrids as multi-potent anti-Alzheimer drug candidates
    • Fang, L., Kraus, B., Lehmann, J., Heilmann, J., Zhang, Y., and Decker, M. (2008) Design and synthesis of tacrine-ferulic acid hybrids as multi-potent anti-Alzheimer drug candidates Bioorg. Med. Chem. Lett. 18, 2905-2909
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 2905-2909
    • Fang, L.1    Kraus, B.2    Lehmann, J.3    Heilmann, J.4    Zhang, Y.5    Decker, M.6
  • 9
    • 84862279415 scopus 로고    scopus 로고
    • Tacrine-silibinin codrug shows neuro- and hepatoprotective effects in vitro and pro-cognitive and hepatoprotective effects in vivo
    • Chen, X., Zenger, K., Lupp, A., Kling, B., Heilmann, J., Fleck, C., Kraus, B., and Decker, M. (2012) Tacrine-silibinin codrug shows neuro- and hepatoprotective effects in vitro and pro-cognitive and hepatoprotective effects in vivo J. Med. Chem. 55, 5231-5242
    • (2012) J. Med. Chem. , vol.55 , pp. 5231-5242
    • Chen, X.1    Zenger, K.2    Lupp, A.3    Kling, B.4    Heilmann, J.5    Fleck, C.6    Kraus, B.7    Decker, M.8
  • 10
    • 58149087995 scopus 로고    scopus 로고
    • NO-donating tacrine hybrid compounds improve scopolamine-induced cognition impairment and show less hepatotoxicity
    • Fang, L., Appenroth, D., Decker, M., Kiehntopf, M., Lupp, A., Peng, S., Fleck, C., Zhang, Y., and Lehmann, J. (2008) NO-donating tacrine hybrid compounds improve scopolamine-induced cognition impairment and show less hepatotoxicity J. Med. Chem. 51, 7666-7669
    • (2008) J. Med. Chem. , vol.51 , pp. 7666-7669
    • Fang, L.1    Appenroth, D.2    Decker, M.3    Kiehntopf, M.4    Lupp, A.5    Peng, S.6    Fleck, C.7    Zhang, Y.8    Lehmann, J.9
  • 11
    • 28744444023 scopus 로고    scopus 로고
    • Structural insights into conformational flexibility at the peripheral site and within the active center gorge of AChE
    • Bourne, Y., Radic, Z., Kolb, H. C., Sharpless, B., Taylor, P., and Marchot, P. (2005) Structural insights into conformational flexibility at the peripheral site and within the active center gorge of AChE Chem.-Biol. Interact. 157, 159-165
    • (2005) Chem.-Biol. Interact. , vol.157 , pp. 159-165
    • Bourne, Y.1    Radic, Z.2    Kolb, H.C.3    Sharpless, B.4    Taylor, P.5    Marchot, P.6
  • 12
    • 78650603475 scopus 로고    scopus 로고
    • Conformational remodeling of femtomolar inhibitor - Acetylcholinesterase complexes in the crystalline state
    • Bourne, Y., Radic, Z., Taylor, P., and Marchot, P. (2010) Conformational remodeling of femtomolar inhibitor-acetylcholinesterase complexes in the crystalline state J. Am. Chem. Soc. 132, 18292-18300
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 18292-18300
    • Bourne, Y.1    Radic, Z.2    Taylor, P.3    Marchot, P.4
  • 14
    • 55249106710 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibitors as disease-modifying therapies for Alzheimer's disease
    • Muñoz-Torrero, D. (2008) Acetylcholinesterase inhibitors as disease-modifying therapies for Alzheimer's disease Curr. Med. Chem. 15, 2433-2455
    • (2008) Curr. Med. Chem. , vol.15 , pp. 2433-2455
    • Muñoz-Torrero, D.1
  • 16
    • 38849194122 scopus 로고    scopus 로고
    • Regulating enzymatic activity with a photoswitchable affinity label
    • Harvey, J. H. and Trauner, D. (2008) Regulating enzymatic activity with a photoswitchable affinity label ChemBioChem 9, 191-193
    • (2008) ChemBioChem , vol.9 , pp. 191-193
    • Harvey, J.H.1    Trauner, D.2
  • 18
    • 84864779538 scopus 로고    scopus 로고
    • Exploring the pharmacology and action spectra of photochromic open-channel blockers
    • Fehrentz, T., Kuttruff, C. A., Huber, F. M. E., Kienzler, M. A., Mayer, P., and Trauner, D. (2012) Exploring the pharmacology and action spectra of photochromic open-channel blockers ChemBioChem 13, 1746-1749
    • (2012) ChemBioChem , vol.13 , pp. 1746-1749
    • Fehrentz, T.1    Kuttruff, C.A.2    Huber, F.M.E.3    Kienzler, M.A.4    Mayer, P.5    Trauner, D.6
  • 19
    • 0348080703 scopus 로고    scopus 로고
    • Diarylethenes for memories and switches
    • Irie, M. (2000) Diarylethenes for memories and switches Chem. Rev. 100, 1685-1716
    • (2000) Chem. Rev. , vol.100 , pp. 1685-1716
    • Irie, M.1
  • 20
    • 33746734322 scopus 로고    scopus 로고
    • Biologically active molecules with a "light switch"
    • Mayer, G. and Heckel, A. (2006) Biologically active molecules with a "light switch" Angew. Chem., Int. Ed. 45, 4900-4921
    • (2006) Angew. Chem., Int. Ed. , vol.45 , pp. 4900-4921
    • Mayer, G.1    Heckel, A.2
  • 21
    • 54749156970 scopus 로고    scopus 로고
    • Regulation of human carbonic anhydrase i (hCAI) activity by using a photochromic inhibitor
    • Vomasta, D., Högner, C., Branda, N. R., and König, B. (2008) Regulation of human carbonic anhydrase I (hCAI) activity by using a photochromic inhibitor Angew. Chem., Int. Ed. 47, 7644-7647
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 7644-7647
    • Vomasta, D.1    Högner, C.2    Branda, N.R.3    König, B.4
  • 22
    • 60449084598 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors: Two-prong versus mono-prong inhibitors of isomers I, II, IX, and XII exemplified by photochromic cis -1,2-α- dithienylethene derivatives
    • Vomasta, D., Innocenti, A., König, B., and Supuran, C. T. (2009) Carbonic anhydrase inhibitors: two-prong versus mono-prong inhibitors of isomers I, II, IX, and XII exemplified by photochromic cis -1,2-α-dithienylethene derivatives Bioorg. Med. Chem. Lett. 19, 1283-1286
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 1283-1286
    • Vomasta, D.1    Innocenti, A.2    König, B.3    Supuran, C.T.4
  • 25
    • 84894129042 scopus 로고    scopus 로고
    • Photopharmacology: Beyond proof of principle
    • For review, see: () - 2191
    • For review, see: Velema, W. A., Szymanski, W., and Feringa, B. L. (2014) Photopharmacology: beyond proof of principle J. Am. Chem. Soc. 136, 2178-2191
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 2178
    • Velema, W.A.1    Szymanski, W.2    Feringa, B.L.3
  • 26
    • 84877669877 scopus 로고    scopus 로고
    • Light-triggered self-assembly of a dichromonyl compound in water
    • Velema, W. A., Stuart, M. C., Szymanski, W., and Feringa, B. L. (2013) Light-triggered self-assembly of a dichromonyl compound in water Chem. Commun. 49, 5001-5003
    • (2013) Chem. Commun. , vol.49 , pp. 5001-5003
    • Velema, W.A.1    Stuart, M.C.2    Szymanski, W.3    Feringa, B.L.4
  • 27
    • 84879048977 scopus 로고    scopus 로고
    • Design, synthesis, and inhibitory activity of potent, photoswitchable mast cell activation inhibitors
    • Velema, W. A., Van der Toorn, M., Szymanski, W., and Feringa, B. L. (2013) Design, synthesis, and inhibitory activity of potent, photoswitchable mast cell activation inhibitors J. Med. Chem. 56, 4456-4464
    • (2013) J. Med. Chem. , vol.56 , pp. 4456-4464
    • Velema, W.A.1    Van Der Toorn, M.2    Szymanski, W.3    Feringa, B.L.4
  • 29
    • 0034635805 scopus 로고    scopus 로고
    • A facile synthesis of bis-tacrine isosteres
    • Hu, M.-K. and Lu, C.-F. (2000) A facile synthesis of bis-tacrine isosteres Tetrahedron Lett. 41, 1815-1818
    • (2000) Tetrahedron Lett. , vol.41 , pp. 1815-1818
    • Hu, M.-K.1    Lu, C.-F.2
  • 30
    • 1342321922 scopus 로고    scopus 로고
    • Tetrahydroacridin-9-ones, 9-chlorotetrahydroacridines, 9-amino-tetrahydroacridines and 9-(pyrazol-1-yl)-tetrahydroacridines derived from chiral cyclanones
    • Frideling, A., Faure, R., Galy, J.-P., Kenz, A., Alkorta, I., and Elguero, J. (2004) Tetrahydroacridin-9-ones, 9-chlorotetrahydroacridines, 9-amino-tetrahydroacridines and 9-(pyrazol-1-yl)-tetrahydroacridines derived from chiral cyclanones Eur. J. Med. Chem. 39, 37-48
    • (2004) Eur. J. Med. Chem. , vol.39 , pp. 37-48
    • Frideling, A.1    Faure, R.2    Galy, J.-P.3    Kenz, A.4    Alkorta, I.5    Elguero, J.6
  • 35
    • 79551469089 scopus 로고    scopus 로고
    • Probing the mid-gorge of cholinesterases with spacer-modified bivalent quinazolinimines leads to highly potent and selective butyrylcholinesterase inhibitors
    • Chen, X., Tikhonova, I. G., and Decker, M. (2011) Probing the mid-gorge of cholinesterases with spacer-modified bivalent quinazolinimines leads to highly potent and selective butyrylcholinesterase inhibitors Bioorg. Med. Chem. 19, 1222-1235
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 1222-1235
    • Chen, X.1    Tikhonova, I.G.2    Decker, M.3
  • 36
    • 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, M. L., Cavalli, A., Melchiorre, C., and 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, M.L.3    Cavalli, A.4    Melchiorre, C.5    Andrisano, V.6
  • 39
    • 80054943835 scopus 로고    scopus 로고
    • DSX: A Knowledge-Based Scoring Function for the Assessment of Protein-Ligand Complexes
    • Neudert, G. and Klebe, G. (2011) DSX: A Knowledge-Based Scoring Function for the Assessment of Protein-Ligand Complexes J. Chem. Inf. Model. 51, 2731-2745
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 2731-2745
    • Neudert, G.1    Klebe, G.2
  • 40
    • 33748544640 scopus 로고    scopus 로고
    • Complexes of Alkylene-Linked Tacrine Dimers with Torpedo californica Acetylcholinesterase: Binding of Bis(5)-tacrine Produces a Dramatic Rearrangement in the Active-Site Gorge
    • Rydberg, E. H., Brumshtein, B., Greenblatt, H. M., Wong, D. M., Shaya, D., Williams, L. D., Carlier, P. R., Pang, Y.-P., Silman, I., and Sussman, J. L. (2006) Complexes of Alkylene-Linked Tacrine Dimers with Torpedo californica Acetylcholinesterase: Binding of Bis(5)-tacrine Produces a Dramatic Rearrangement in the Active-Site Gorge J. Med. Chem. 49, 5491-5500
    • (2006) J. Med. Chem. , vol.49 , pp. 5491-5500
    • Rydberg, E.H.1    Brumshtein, B.2    Greenblatt, H.M.3    Wong, D.M.4    Shaya, D.5    Williams, L.D.6    Carlier, P.R.7    Pang, Y.-P.8    Silman, I.9    Sussman, J.L.10
  • 41
    • 32044459019 scopus 로고    scopus 로고
    • Novel tricyclic quinazolinimines and related tetracyclic nitrogen bridgehead compounds as cholinesterase inhibitors with selectivity towards butyrylcholinesterase
    • Decker, M., Krauth, F., and Lehmann, J. (2006) Novel tricyclic quinazolinimines and related tetracyclic nitrogen bridgehead compounds as cholinesterase inhibitors with selectivity towards butyrylcholinesterase Bioorg. Med. Chem. 14, 1966-1977
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 1966-1977
    • Decker, M.1    Krauth, F.2    Lehmann, J.3
  • 43
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: The European molecular biology open software suite
    • Rice, P., Longden, I., and Bleasby, A. (2000) EMBOSS: the European molecular biology open software suite Trends Genet. 16, 276-277
    • (2000) Trends Genet. , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 44
    • 84901265927 scopus 로고    scopus 로고
    • CCDC Software
    • GOLDSUITE 5.1, CCDC Software, www.ccdc.cam.ac.uk.
    • GOLDSUITE 5.1
  • 46
    • 84855757480 scopus 로고    scopus 로고
    • 2011.10, Chemical Computing Group Inc. 1010 Sherbooke St. West, Suite #910, Montreal, QC, Canada, H3A 2R7
    • Molecular Operating Environment (MOE), 2011.10, Chemical Computing Group Inc., 1010 Sherbooke St. West, Suite #910, Montreal, QC, Canada, H3A 2R7, 2011.
    • (2011) Molecular Operating Environment (MOE)
  • 47
    • 37249023309 scopus 로고    scopus 로고
    • New and Original p K a Prediction Method Using Grid Molecular Interaction Fields
    • Milletti, F., Storchi, L., Sforna, G., and Cruciani, G. (2007) New and Original p K a Prediction Method Using Grid Molecular Interaction Fields J. Chem. Inf. Model. 47, 2172-2181
    • (2007) J. Chem. Inf. Model. , vol.47 , pp. 2172-2181
    • Milletti, F.1    Storchi, L.2    Sforna, G.3    Cruciani, G.4
  • 48
    • 26444468103 scopus 로고    scopus 로고
    • General and Targeted Statistical Potentials for Protein-Ligand Interactions
    • Mooij, W. T. M. and Verdonk, M. L. (2005) General and Targeted Statistical Potentials for Protein-Ligand Interactions Proteins 61, 272-287
    • (2005) Proteins , vol.61 , pp. 272-287
    • Mooij, W.T.M.1    Verdonk, M.L.2
  • 50
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: The RESP model
    • Bayly, C. I., Cieplak, P., Cornell, W., and Kollman, P. A. (1993) A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP model J. Phys. Chem. 97, 10269-10280
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.3    Kollman, P.A.4
  • 53
    • 33748538349 scopus 로고    scopus 로고
    • Automatic atom type and bond type perception in molecular mechanical calculations
    • Wang, J., Wang, W., Kollman, P. A., and Case, D. A. (2006) Automatic atom type and bond type perception in molecular mechanical calculations J. Mol. Graphics Model. 25, 247-260
    • (2006) J. Mol. Graphics Model. , vol.25 , pp. 247-260
    • Wang, J.1    Wang, W.2    Kollman, P.A.3    Case, D.A.4
  • 54
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Šali, A. and Blundell, T. L. (1993) Comparative protein modeling by satisfaction of spatial restraints J. Mol. Biol. 234, 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 55
    • 0344778061 scopus 로고
    • Semianalytical treatment of solvation for molecular mechanics and dynamics
    • Still, W. C., Tempczyk, A., Hawley, R. C., and Hendrickson, T. (1990) Semianalytical treatment of solvation for molecular mechanics and dynamics J. Am. Chem. Soc. 112, 6127-6129
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 6127-6129
    • Still, W.C.1    Tempczyk, A.2    Hawley, R.C.3    Hendrickson, T.4
  • 56
    • 0033468737 scopus 로고    scopus 로고
    • Application of a pairwise generalized Born model to proteins and nucleic acids: Inclusion of salt effects
    • Srinivasan, J., Trevathan, M. W., and Case, D. (1999) Application of a pairwise generalized Born model to proteins and nucleic acids: inclusion of salt effects Theor. Chem. Acc. 101, 426-434
    • (1999) Theor. Chem. Acc. , vol.101 , pp. 426-434
    • Srinivasan, J.1    Trevathan, M.W.2    Case, D.3
  • 59
    • 36449003554 scopus 로고
    • Constant pressure molecular dynamics algorithms
    • Martyna, G. J., Tobias, D. J., and Klein, M. L. (1994) Constant pressure molecular dynamics algorithms J. Chem. Phys. 101, 4177-4189
    • (1994) J. Chem. Phys. , vol.101 , pp. 4177-4189
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3
  • 60
    • 36449007836 scopus 로고
    • Constant-pressure molecular-dynamics simulation-the Langevin piston method
    • Feller, S. E., Zhang, Y., Pastor, R. W., and Brooks, B. R. (1995) Constant-pressure molecular-dynamics simulation-the Langevin piston method J. Chem. Phys. 103, 4613-4621
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.R.4
  • 61
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N.Log(N) method for Ewald sums in large systems
    • Darden, T., York, D., and Pedersen, L. (1993) Particle mesh Ewald: an N.Log(N) method for Ewald sums in large systems J. Chem. Phys. 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 63
    • 84863304598 scopus 로고    scopus 로고
    • R Core Team (), R Foundation for Statistical Computing, Vienna, Austria, ISBN 3-900051-07-0
    • R Core Team (2013) R: A language and environment for statistical computing, R Foundation for Statistical Computing, Vienna, Austria, ISBN 3-900051-07-0, http://www.R-project.org/.
    • (2013) R: A Language and Environment for Statistical Computing


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.