메뉴 건너뛰기




Volumn 84, Issue , 2014, Pages 107-117

Tetrahydrobenzo[h][1,6]naphthyridine-6-chlorotacrine hybrids as a new family of anti-Alzheimer agents targeting β-amyloid, tau, and cholinesterase pathologies

Author keywords

A aggregation inhibitors; Dual binding site AChE inhibitors; Multitarget compounds; Tau aggregation inhibitors; Tetrahydrobenzo h 1,6 naphthyridines

Indexed keywords

ACETYLCHOLINESTERASE; AMIDE; AMYLOID BETA PROTEIN[1-42]; CENTRAL NERVOUS SYSTEM AGENTS; CHOLINESTERASE; N [3 [(6 CHLORO 1,2,3,4 TETRAHYDROACRIDIN 9 YL)AMINO]PROPYL] 5 (4 CHLOROPHENYL) 1,2,3,4 TETRAHYDROBENZO[H][1,6]NAPHTHYRIDINE 9 CARBOXAMIDE; N [4 [(6 CHLORO 1,2,3,4 TETRAHYDROACRIDIN 9 YL)AMINO]BUTYL] 5 (4 CHLOROPHENYL) 1,2,3,4 TETRAHYDROBENZO[H][1,6]NAPHTHYRIDINE 9 CARBOXAMIDE; N [5 [(6 CHLORO 1,2,3,4 TETRAHYDROACRIDIN 9 YL)AMINO]PENTYL] 5 (4 CHLOROPHENYL) 1,2,3,4 TETRAHYDROBENZO[H][1,6]NAPHTHYRIDINE 9 CARBOXAMIDE; N [8 [(6 CHLORO 1,2,3,4 TETRAHYDROACRIDIN 9 YL)AMINO]OCTYL] 5 (4 CHLOROPHENYL) 1,2,3,4 TETRAHYDROBENZO[H][1,6]NAPHTHYRIDINE 9 CARBOXAMIDE; NAPHTHYRIDINE DERIVATIVE; TACRINE; TAU PROTEIN; TETRAHYDROBENZO[H][1,6]NAPHTHYRIDINE 6 CHLOROTACRINE; UNCLASSIFIED DRUG; 6 CHLOROTACRINE; CHOLINESTERASE INHIBITOR; AMYLOID BETA PROTEIN; N-(3-((6-CHLORO-1,2,3,4-TETRAHYDROACRIDIN-9-YL)AMINO)PROPYL)-5-(4-CHLOROPHENYL)-1,2,3,4-TETRAHYDROBENZO(H)(1,6)NAPHTHYRIDINE-9-CARBOXAMIDE;

EID: 84904170030     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2014.07.021     Document Type: Article
Times cited : (65)

References (57)
  • 1
    • 84875354777 scopus 로고    scopus 로고
    • Alzheimer's disease facts and figures
    • Alzheimer's Association Alzheimer's disease facts and figures Alzheimers Dement. 9 2013 208 245
    • (2013) Alzheimers Dement. , vol.9 , pp. 208-245
    • Association, A.1
  • 3
    • 60349125886 scopus 로고    scopus 로고
    • Reassessing the amyloid cascade hypothesis of Alzheimer's disease
    • S.W. Pimplikar Reassessing the amyloid cascade hypothesis of Alzheimer's disease Int. J. Biochem. Cell. Biol. 41 2009 1261 1268
    • (2009) Int. J. Biochem. Cell. Biol. , vol.41 , pp. 1261-1268
    • Pimplikar, S.W.1
  • 4
    • 84896736436 scopus 로고    scopus 로고
    • Multifunctional compounds: Smart molecules for multifactorial diseases
    • Y. Bansal, and O. Silakari Multifunctional compounds: smart molecules for multifactorial diseases Eur. J. Med. Chem. 76 2014 31 42
    • (2014) Eur. J. Med. Chem. , vol.76 , pp. 31-42
    • Bansal, Y.1    Silakari, O.2
  • 5
    • 84877948856 scopus 로고    scopus 로고
    • Rationally designed multi-targeted agents against neurodegenerative diseases
    • W.J. Geldenhuys, and C.J. Van der Schyf Rationally designed multi-targeted agents against neurodegenerative diseases Curr. Med. Chem. 20 2013 1662 1672
    • (2013) Curr. Med. Chem. , vol.20 , pp. 1662-1672
    • Geldenhuys, W.J.1    Van Der Schyf, C.J.2
  • 6
    • 84877982789 scopus 로고    scopus 로고
    • Multi-target compounds acting in the central nervous system designed from natural products
    • X. Chen, and M. Decker Multi-target compounds acting in the central nervous system designed from natural products Curr. Med. Chem. 20 2013 1673 1685
    • (2013) Curr. Med. Chem. , vol.20 , pp. 1673-1685
    • Chen, X.1    Decker, M.2
  • 8
    • 82055186741 scopus 로고    scopus 로고
    • Hybrid-based multi-target ligands for the treatment of Alzheimer's disease
    • A. Rampa, F. Belluti, S. Gobbi, and A. Bisi Hybrid-based multi-target ligands for the treatment of Alzheimer's disease Curr. Top. Med. Chem. 11 2011 2716 2730
    • (2011) Curr. Top. Med. Chem. , vol.11 , pp. 2716-2730
    • Rampa, A.1    Belluti, F.2    Gobbi, S.3    Bisi, A.4
  • 10
    • 84866122213 scopus 로고    scopus 로고
    • Sting of Alzheimer's failures offset by upcoming prevention trials
    • A. Mullard Sting of Alzheimer's failures offset by upcoming prevention trials Nat. Rev. Drug. Discov. 11 2012 657 660
    • (2012) Nat. Rev. Drug. Discov. , vol.11 , pp. 657-660
    • Mullard, A.1
  • 11
    • 84890528022 scopus 로고    scopus 로고
    • Biomarker modeling of Alzheimer's disease
    • C.R. Jack Jr., and D.M. Holtzman Biomarker modeling of Alzheimer's disease Neuron 80 2013 1347 1358
    • (2013) Neuron , vol.80 , pp. 1347-1358
    • Jack, Jr.C.R.1    Holtzman, D.M.2
  • 12
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme
    • DOI 10.1016/S0896-6273(00)80108-7
    • N.C. Inestrosa, A. Alvarez, C.A. Pérez, R.D. Moreno, M. Vicente, C. Linker, O.I. Casanueva, C. Soto, and J. Garrido Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme Neuron 16 1996 881 891 (Pubitemid 26124065)
    • (1996) Neuron , vol.16 , Issue.4 , 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
  • 13
    • 38549098085 scopus 로고    scopus 로고
    • Amyloid-cholinesterase interactions: Implications for Alzheimer's disease
    • DOI 10.1111/j.1742-4658.2007.06238.x
    • N.C. Inestrosa, M.C. Dinamarca, and A. Alvarez Amyloid-cholinesterase interactions. Implications for Alzheimer's disease FEBS J. 275 2008 625 632 (Pubitemid 351160969)
    • (2008) FEBS Journal , vol.275 , Issue.4 , pp. 625-632
    • Inestrosa, N.C.1    Dinamarca, M.C.2    Alvarez, A.3
  • 14
    • 0035807054 scopus 로고    scopus 로고
    • A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation
    • DOI 10.1021/bi0101392
    • G.V. De Ferrari, M.A. Canales, I. Shin, L.M. Weiner, I. Silman, and N.C. Inestrosa A structural motif of acetylcholinesterase that promotes amyloid beta-peptide fibril formation Biochemistry 40 2001 10447 10457 (Pubitemid 32816655)
    • (2001) Biochemistry , vol.40 , Issue.35 , pp. 10447-10457
    • De Ferrari, G.V.1    Canales, M.A.2    Shin, I.3    Weiner, L.M.4    Silman, I.5    Inestrosa, N.C.6
  • 15
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • J.L. Sussman, M. Harel, F. Frolow, C. Oefner, A. Goldman, L. Toker, and I. Silman Atomic structure of acetylcholinesterase from Torpedo californica - a prototypic acetylcholine-binding protein Science 253 1991 872 879 (Pubitemid 21917225)
    • (1991) Science , vol.253 , Issue.5022 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 19
    • 76849089003 scopus 로고    scopus 로고
    • Unsaturated lactams: New inputs for Povarov-type multicomponent reactions
    • E. Vicente-García, F. Catti, R. Ramón, and R. Lavilla Unsaturated lactams: new inputs for Povarov-type multicomponent reactions Org. Lett. 12 2010 860 863
    • (2010) Org. Lett. , vol.12 , pp. 860-863
    • Vicente-García, E.1    Catti, F.2    Ramón, R.3    Lavilla, R.4
  • 20
    • 79960402602 scopus 로고    scopus 로고
    • Multicomponent reaction access to complex quinolines via oxidation of the Povarov adducts
    • E. Vicente-García, R. Ramón, S. Preciado, and R. Lavilla Multicomponent reaction access to complex quinolines via oxidation of the Povarov adducts Beilstein J. Org. Chem. 7 2011 980 987
    • (2011) Beilstein J. Org. Chem. , vol.7 , pp. 980-987
    • Vicente-García, E.1    Ramón, R.2    Preciado, S.3    Lavilla, R.4
  • 25
    • 0037087516 scopus 로고    scopus 로고
    • Click chemistry in situ: Acetylcholinesterase as a reaction vessel for the selective assembly of a femtomolar inhibitor from an array of building blocks
    • DOI 10.1002/1521-3773(20020315)41:6<1053::AID-ANIE1053>3.0.CO;2-4
    • W.G. Lewis, L.G. Green, F. Grynszpan, Z. Radić, P.R. Carlier, P. Taylor, M.G. Finn, and K.B. Sharpless Click chemistry in situ: acetylcholinesterase as a reaction vessel for the selective assembly of a femtomolar inhibitor from an array of building blocks Angew. Chem. Int. Ed. 41 2002 1053 1057 (Pubitemid 34251912)
    • (2002) Angewandte Chemie - International Edition , vol.41 , Issue.6 , pp. 1053-1057
    • Lewis, W.G.1    Green, L.G.2    Grynszpan, F.3    Radic, Z.4    Carlier, P.R.5    Taylor, P.6    Finn, M.G.7    Sharpless, K.B.8
  • 26
    • 0033966913 scopus 로고    scopus 로고
    • Huprine X is a novel high-affinity inhibitor of acetylcholinesterase that is of interest for treatment of Alzheimer's disease
    • P. Camps, B. Cusack, W.D. Mallender, R. El Achab, J. Morral, D. Muñoz-Torrero, and T.L. Rosenberry Huprine X is a novel high-affinity inhibitor of acetylcholinesterase that is of interest for the treatment of Alzheimer's disease Mol. Pharmacol. 57 2000 409 417 (Pubitemid 30084519)
    • (2000) Molecular Pharmacology , vol.57 , Issue.2 , pp. 409-417
    • Camps, P.1    Cusack, B.2    Mallender, W.D.3    El Achab, R.4    Morral, J.5    Munoz-Torrero, D.6    Rosenberry, T.L.7
  • 27
    • 84880070992 scopus 로고    scopus 로고
    • Crystal structures of human cholinesterases in complex with huprine W and tacrine: Elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyrylcholinesterase
    • F. Nachon, E. Carletti, C. Ronco, M. Trovaslet, Y. Nicolet, L. Jean, and P.-Y. Renard Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyrylcholinesterase Biochem. J. 453 2013 393 399
    • (2013) Biochem. J. , vol.453 , pp. 393-399
    • Nachon, F.1    Carletti, E.2    Ronco, C.3    Trovaslet, M.4    Nicolet, Y.5    Jean, L.6    Renard, P.-Y.7
  • 28
    • 0037022789 scopus 로고    scopus 로고
    • 3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: Kinetic and molecular dynamic correlates
    • DOI 10.1021/bi011652i
    • H. Dvir, D.M. Wong, M. Harel, X. Barril, M. Orozco, F.J. Luque, D. Muñoz-Torrero, P. Camps, T.L. Rosenberry, I. Silman, and J.L. Sussman 3D Structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 Å resolution: kinetic and molecular dynamics correlates Biochemistry 41 2002 2970 2981 (Pubitemid 34184628)
    • (2002) Biochemistry , vol.41 , Issue.9 , pp. 2970-2981
    • Dvir, H.1    Wong, D.M.2    Harel, M.3    Barril, X.4    Orozco, M.5    Luque, F.J.6    Munoz-Torrero, D.7    Camps, P.8    Rosenberry, T.L.9    Silman, I.10    Sussman, J.L.11
  • 30
    • 30344485665 scopus 로고    scopus 로고
    • Targeting acetylcholinesterase and butyrylcholinesterase in dementia
    • DOI 10.1017/S1461145705005833, PII S1461145705005833
    • R.M. Lane, S.G. Potkin, and A. Enz Targeting acetylcholinesterase and butyrylcholinesterase in dementia Int. J. Neuropsychopharmacol. 9 2006 101 124 (Pubitemid 43068340)
    • (2006) International Journal of Neuropsychopharmacology , vol.9 , Issue.1 , pp. 101-124
    • Lane, R.M.1    Potkin, S.G.2    Enz, A.3
  • 31
    • 84887887445 scopus 로고    scopus 로고
    • Dual inhibitors of β-amyloid aggregation and acetylcholinesterase as multi-target anti-Alzheimer drug candidates
    • E. Viayna, R. Sabate, and D. Muñoz-Torrero Dual inhibitors of β-amyloid aggregation and acetylcholinesterase as multi-target anti-Alzheimer drug candidates Curr. Top. Med. Chem. 13 2013 1820 1842
    • (2013) Curr. Top. Med. Chem. , vol.13 , pp. 1820-1842
    • Viayna, E.1    Sabate, R.2    Muñoz-Torrero, D.3
  • 33
    • 84896335260 scopus 로고    scopus 로고
    • Thioflavin-S staining of bacterial inclusion bodies for the fast, simple, and inexpensive screening of amyloid aggregation inhibitors
    • S. Pouplana, A. Espargaró, C. Galdeano, E. Viayna, I. Sola, S. Ventura, D. Muñoz-Torrero, and R. Sabate Thioflavin-S staining of bacterial inclusion bodies for the fast, simple, and inexpensive screening of amyloid aggregation inhibitors Curr. Med. Chem. 21 2014 1152 1159
    • (2014) Curr. Med. Chem. , vol.21 , pp. 1152-1159
    • Pouplana, S.1    Espargaró, A.2    Galdeano, C.3    Viayna, E.4    Sola, I.5    Ventura, S.6    Muñoz-Torrero, D.7    Sabate, R.8
  • 34
    • 33745096194 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism
    • DOI 10.1111/j.1747-0285.2005.00318.x
    • Y. Porat, A. Abramowitz, and E. Gazit Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism Chem. Biol. Drug. Des. 67 2006 27 37 (Pubitemid 43881385)
    • (2006) Chemical Biology and Drug Design , vol.67 , Issue.1 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 36
    • 84889610430 scopus 로고    scopus 로고
    • Past and recent progress of molecular imaging probes for β-amyloid plaques in the brain
    • M. Cui Past and recent progress of molecular imaging probes for β-amyloid plaques in the brain Curr. Med. Chem. 21 2014 82 112
    • (2014) Curr. Med. Chem. , vol.21 , pp. 82-112
    • Cui, M.1
  • 38
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • DOI 10.1016/S0169-409X(96)00423-1, PII S0169409X96004231
    • C.A. Lipinski, F. Lombardo, B.W. Dominy, and P.J. Feeney Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings Adv. Drug. Deliv. Rev. 23 1997 3 25 (Pubitemid 27046991)
    • (1997) Advanced Drug Delivery Reviews , vol.23 , Issue.1-3 , pp. 3-25
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 39
    • 65549171659 scopus 로고    scopus 로고
    • Designing multiple ligands - Medicinal chemistry strategies and challenges
    • R. Morphy, and Z. Rankovic Designing multiple ligands - medicinal chemistry strategies and challenges Curr. Pharm. Des. 15 2009 587 600
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 587-600
    • Morphy, R.1    Rankovic, Z.2
  • 41
    • 77953936624 scopus 로고    scopus 로고
    • A new tacrine-melatonin hybrid reduces amyloid burden and behavioral deficits in a mouse model of Alzheimer's disease
    • C. Spuch, D. Antequera, M.I. Fernandez-Bachiller, M.I. Rodríguez-Franco, and E. Carro A new tacrine-melatonin hybrid reduces amyloid burden and behavioral deficits in a mouse model of Alzheimer's disease Neurotox. Res. 17 2010 421 431
    • (2010) Neurotox. Res. , vol.17 , pp. 421-431
    • Spuch, C.1    Antequera, D.2    Fernandez-Bachiller, M.I.3    Rodríguez-Franco, M.I.4    Carro, E.5
  • 45
    • 84962359573 scopus 로고    scopus 로고
    • High throughput artificial membrane permeability assay for blood-brain barrier
    • DOI 10.1016/S0223-5234(03)00012-6
    • L. Di, E.H. Kerns, K. Fan, O.J. McConnell, and G.T. Carter High throughput artificial membrane permeability assay for blood-brain barrier Eur. J. Med. Chem. 38 2003 223 232 (Pubitemid 36349665)
    • (2003) European Journal of Medicinal Chemistry , vol.38 , Issue.3 , pp. 223-232
    • Di, L.1    Kerns, E.H.2    Fan, K.3    McConnell, O.J.4    Carter, G.T.5
  • 47
    • 0029099970 scopus 로고
    • 5,7-Dihydro-3-[2-[1-(phenylmethyl)-4-piperidinyl]ethyl]-6H-pyrrolo[3,2-f] -1,2-benzisoxazol-6-one: A potent and centrally-selective inhibitor of acetylcholinesterase
    • A. Villalobos, T.W. Butler, D.S. Chapin, Y.L. Chen, S.B. DeMattos, J.L. Ives, S.B. Jones, D.R. Liston, and A.A. Nagel 5,7-Dihydro-3-[2-[1-(phenylmethyl) -4-piperidinyl]ethyl]-6H-pyrrolo[3,2-f]-1,2-benzisoxazol-6-one: a potent and centrally-selective inhibitor of acetylcholinesterase J. Med. Chem. 38 1995 2802 2808
    • (1995) J. Med. Chem. , vol.38 , pp. 2802-2808
    • Villalobos, A.1    Butler, T.W.2    Chapin, D.S.3    Chen, Y.L.4    Demattos, S.B.5    Ives, J.L.6    Jones, S.B.7    Liston, D.R.8    Nagel, A.A.9
  • 50
    • 79951476387 scopus 로고    scopus 로고
    • PROPKA3: Consistent treatment of internal and surface residues in empirical pKa predictions
    • M.H.M. Olsson, C.R. Sondergard, M. Rostkowski, and J.H. Jensen PROPKA3: consistent treatment of internal and surface residues in empirical pKa predictions J. Chem. Theory Comput. 7 2011 525 537
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 525-537
    • Olsson, M.H.M.1    Sondergard, C.R.2    Rostkowski, M.3    Jensen, J.H.4
  • 54
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • A.D. Becke Density-functional thermochemistry. III. The role of exact exchange J. Chem. Phys. 98 1993 5648 5652
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 55
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
    • C. Lee, W. Yang, and R.G. Parr Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density Phys. Rev. B 37 1988 785 789
    • (1988) Phys. Rev. B , vol.37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 56
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges
    • C.I. Bayly, P. Cieplak, W.D. Cornell, and P.A. Kollman A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges J. Phys. Chem. 97 1993 10269 10280
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.