Base de dados : MEDLINE
Pesquisa : B01.050.150.900.493.378.430.250 [Categoria DeCS]
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[PMID]:29353726
[Au] Autor:Czarnecka K; Chufarova N; Halczuk K; Maciejewska K; Girek M; Skibinski R; Jonczyk J; Bajda M; Kabzinski J; Majsterek I; Szymanski P
[Ad] Endereço:Department of Pharmaceutical Chemistry, Drug Analyses and Radiopharmacy, Faculty of Pharmacy, Medical University of Lodz, Muszynskiego 1, 90-151 Lodz, Poland. Electronic address: kamila.czarnecka@umed.lodz.pl.
[Ti] Título:Tetrahydroacridine derivatives with dichloronicotinic acid moiety as attractive, multipotent agents for Alzheimer's disease treatment.
[So] Source:Eur J Med Chem;145:760-769, 2018 Feb 10.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:A novel series of 9-amino-1,2,3,4-tetrahydroacridine and 5,6-dichloronicotinic acid moiety were conjugated with different linkers. Afterwards new derivatives were evaluated as potential multifunctional acetylcholinesterase inhibitors (AChEIs), anti-Alzheimer's disease (AD) drug candidates. All the compounds were synthesized and tested for capacity for the inhibition of acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) enzymes. Specifically, the most promising derivative 3b (IC = 1.02 nM) had higher inhibitory potency compared to the reference drug, tacrine. Consequently, kinetic studies of 3b compound showed a mixed-type inhibition of both AChE and BuChE. Afterwards the best potent AChE inhibitor has been examined on amyloid ß (Aß) self-induced aggregation. Furthermore, 3b compound was tested in various concentrations and had moderate activity against Aß aggregation. Inhibition of Aß aggregation was 46.63% and 19.41% at 50 µM and 5  µM concentrations, respectively. Moreover, no cytotoxicity was observed for the mentioned concentrations. Therefore, 3b compound is a promising multipotent agent for the treatment of AD.
[Mh] Termos MeSH primário: Acetilcolinesterase/metabolismo
Acridinas/farmacologia
Doença de Alzheimer/tratamento farmacológico
Butirilcolinesterase/metabolismo
Inibidores da Colinesterase/farmacologia
Ácidos Nicotínicos/farmacologia
[Mh] Termos MeSH secundário: Acridinas/química
Doença de Alzheimer/metabolismo
Peptídeos beta-Amiloides/antagonistas & inibidores
Peptídeos beta-Amiloides/metabolismo
Animais
Inibidores da Colinesterase/síntese química
Inibidores da Colinesterase/química
Relação Dose-Resposta a Droga
Electrophorus
Cavalos
Seres Humanos
Modelos Moleculares
Estrutura Molecular
Ácidos Nicotínicos/química
Relação Estrutura-Atividade
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5,6-dichloronicotinic acid); 0 (Acridines); 0 (Amyloid beta-Peptides); 0 (Cholinesterase Inhibitors); 0 (Nicotinic Acids); EC 3.1.1.7 (Acetylcholinesterase); EC 3.1.1.8 (Butyrylcholinesterase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180123
[St] Status:MEDLINE


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[PMID]:29324339
[Au] Autor:Azzouz R; Peauger L; Gembus V; Tîntas ML; Sopková-de Oliveira Santos J; Papamicaël C; Levacher V
[Ad] Endereço:VFP Therapies, 15 rue François Couperin, 76000 Rouen, France.
[Ti] Título:Novel donepezil-like N-benzylpyridinium salt derivatives as AChE inhibitors and their corresponding dihydropyridine "bio-oxidizable" prodrugs: Synthesis, biological evaluation and structure-activity relationship.
[So] Source:Eur J Med Chem;145:165-190, 2018 Feb 10.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:As an extension of our previous work on donepezil-based "bio-oxidizable" prodrug approach, two new classes of N-benzylpyridinium donepezil analogues in tetralone B2 and acetophenone B3 series and a new set of indanone derivatives B1 were investigated along with the corresponding dihydropyridine prodrugs A1-3. A total of fifty one N-benzylpyridinium quaternary donepezil analogues B1-3 and twenty two prodrugs A1-3 were synthesized and evaluated for their inhibitory activities against hAChE and eqBuChE. While most prodrugs A1-3 were demonstrated to be inactive against AChE (IC > 10 µM), a large number of the corresponding N-benzylpyridinium salt B1-3 exhibited appealing three-to-one-digit nanomolar hAChE inhibitory activities and even reaching subnanomolar activity (IC = 0.36 nM). In addition, in silico docking studies were conducted for several compounds to explain the more relevant in vitro results. Lastly, the influence of the two stereogenic centers in prodrugs A was also evaluated, highlighting not only marked differences in residual AChE inhibitory activity of the four separated isomers of prodrug 23h (IC ranging from 173 nM to 10 µM) but also significant variations of the oxidation rate between two separated diastereoisomers of prodrug 24a. This work provides useful information in the search of a preclinical candidate to conduct further development of this attractive "bio-oxidizable" prodrug strategy.
[Mh] Termos MeSH primário: Acetilcolinesterase/metabolismo
Inibidores da Colinesterase/farmacologia
Di-Hidropiridinas/farmacologia
Pró-Fármacos/farmacologia
Compostos de Piridínio/farmacologia
[Mh] Termos MeSH secundário: Animais
Butirilcolinesterase/metabolismo
Inibidores da Colinesterase/síntese química
Inibidores da Colinesterase/química
Di-Hidropiridinas/química
Relação Dose-Resposta a Droga
Electrophorus
Cavalos
Simulação de Acoplamento Molecular
Estrutura Molecular
Pró-Fármacos/síntese química
Pró-Fármacos/química
Compostos de Piridínio/síntese química
Compostos de Piridínio/química
Sais/síntese química
Sais/química
Sais/farmacologia
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cholinesterase Inhibitors); 0 (Dihydropyridines); 0 (Prodrugs); 0 (Pyridinium Compounds); 0 (Salts); 7M8K3P6I89 (1,4-dihydropyridine); EC 3.1.1.7 (Acetylcholinesterase); EC 3.1.1.8 (Butyrylcholinesterase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE


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[PMID]:29360451
[Au] Autor:Xu J; Yang F; Han D; Xu S
[Ad] Endereço:Key Laboratory for the Physics & Chemistry of Nanodevices, Department of Electronics, Peking University, Beijing, 100871, PR China.
[Ti] Título:Phenomena of synchronized response in biosystems and the possible mechanism.
[So] Source:Biochem Biophys Res Commun;496(2):661-666, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phenomena of synchronized response is common among organs, tissues and cells in biosystems. We have analyzed and discussed three examples of synchronization in biosystems, including the direction-changing movement of paramecia, the prey behavior of flytraps, and the simultaneous discharge of electric eels. These phenomena and discussions support an electrical communication mechanism that in biosystems, the electrical signals are mainly soliton-like electromagnetic pulses, which are generated by the transient transmembrane ionic current through the ion channels and propagate along the dielectric membrane-based softmaterial waveguide network to complete synchronized responses. This transmission model implies that a uniform electrical communication mechanism might have been naturally developed in biosystem.
[Mh] Termos MeSH primário: Comunicação Animal
Fenômenos Eletrofisiológicos
Canais Iônicos/metabolismo
[Mh] Termos MeSH secundário: Animais
Membrana Celular/metabolismo
Eletricidade
Electrophorus/fisiologia
Transporte de Íons
Movimento
Paramecium/fisiologia
Sarraceniaceae/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ion Channels)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180124
[St] Status:MEDLINE


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[PMID]:29262703
[Au] Autor:Gyori J; Farkas A; Stolyar O; Székács A; Mörtl M; Vehovszky Á
[Ad] Endereço:1 Department of Experimental Zoology, MTA Centre for Ecological Research, Balaton Limnological Institute , H-8237 Tihany, POB 35 , Hungary.
[Ti] Título:Inhibitory effects of four neonicotinoid active ingredients on acetylcholine esterase activity.
[So] Source:Acta Biol Hung;68(4):345-357, 2017 Dec.
[Is] ISSN:0236-5383
[Cp] País de publicação:Hungary
[La] Idioma:eng
[Ab] Resumo:There is a great concern about the decline of pollinators, and neonicotinoids emerging bee disorders are assumed to play a significant role. Since changes in learning ability has been observed in honey bees exposed to some acetylcholine esterase (AChE) inhibitors, we therefore, tested in vitro the effect of four neonicotinoids on purified eel AChE. AChE activity was inhibited in a concentration-dependent manner, and calculated IC values for thiamethoxam (IC = 414 µM) and clothianidin (IC = 160 µM) were found to be much higher compared to acetamiprid (IC = 75.2 µM) and thiacloprid (IC = 87.8 µM). The Lineweaver-Burk reciprocal plots for acetamiprid shows unchanged V and increased K values with inhibitor concentrations, while analysis of Michaelis-Menten plots shows predominantly competitive mechanism. The inhibition constant value (K = 24.3 µM) indicates strong binding of the acetamiprid complex to AChE. Finally, the four tested neonicotinoids are not a uniform group regarding their blocking ability. Our results suggest a previously not established, direct AChE blocking mechanism of neonicotinoids tested, thus the neuronal AChE enzyme is likely among the direct targets of the neonicotinoid insecticides. We conclude, that these AChE inhibitory effects may also contribute to toxic effects on the whole exposed animal.
[Mh] Termos MeSH primário: Acetilcolinesterase/química
Inibidores da Colinesterase/química
Electrophorus
Proteínas de Peixes
Guanidinas/química
Neonicotinoides/química
Nitrocompostos/química
Oxazinas/química
Tiazóis/química
[Mh] Termos MeSH secundário: Animais
Proteínas de Peixes/antagonistas & inibidores
Proteínas de Peixes/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cholinesterase Inhibitors); 0 (Fish Proteins); 0 (Guanidines); 0 (Neonicotinoids); 0 (Nitro Compounds); 0 (Oxazines); 0 (Thiazoles); 2V9906ABKQ (clothianidin); 5HL5N372P0 (acetamiprid); 747IC8B487 (thiamethoxam); EC 3.1.1.7 (Acetylcholinesterase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE
[do] DOI:10.1556/018.68.2017.4.1


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[PMID]:29405075
[Au] Autor:Zhu J; Yang H; Chen Y; Lin H; Li Q; Mo J; Bian Y; Pei Y; Sun H
[Ad] Endereço:a Department of Medicinal Chemistry , China Pharmaceutical University , Nanjing , China.
[Ti] Título:Synthesis, pharmacology and molecular docking on multifunctional tacrine-ferulic acid hybrids as cholinesterase inhibitors against Alzheimer's disease.
[So] Source:J Enzyme Inhib Med Chem;33(1):496-506, 2018 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The cholinergic hypothesis has long been a "polar star" in drug discovery for Alzheimer's disease (AD), resulting in many small molecules and biological drug candidates. Most of the drugs marketed for AD are cholinergic. Herein, we report our efforts in the discovery of cholinesterases inhibitors (ChEIs) as multi-target-directed ligands. A series of tacrine-ferulic acid hybrids have been designed and synthesised. All these compounds showed potent acetyl-(AChE) and butyryl cholinesterase(BuChE) inhibition. Among them, the optimal compound 10g, was the most potent inhibitor against AChE (electrophorus electricus (eeAChE) half maximal inhibitory concentration (IC ) = 37.02 nM), it was also a strong inhibitor against BuChE (equine serum (eqBuChE) IC = 101.40 nM). Besides, it inhibited amyloid ß-protein self-aggregation by 65.49% at 25 µM. In subsequent in vivo scopolamine-induced AD models, compound 10g obviously ameliorated the cognition impairment and showed preliminary safety in hepatotoxicity evaluation. These data suggest compound 10g as a promising multifunctional agent in the drug discovery process against AD.
[Mh] Termos MeSH primário: Doença de Alzheimer/tratamento farmacológico
Inibidores da Colinesterase/síntese química
Inibidores da Colinesterase/farmacologia
Ácidos Cumáricos/farmacologia
Simulação de Acoplamento Molecular
Tacrina/farmacologia
[Mh] Termos MeSH secundário: Acetilcolinesterase/metabolismo
Doença de Alzheimer/induzido quimicamente
Peptídeos beta-Amiloides/antagonistas & inibidores
Animais
Butirilcolinesterase/metabolismo
Inibidores da Colinesterase/química
Ácidos Cumáricos/química
Relação Dose-Resposta a Droga
Electrophorus
Cavalos
Seres Humanos
Ligantes
Masculino
Camundongos
Camundongos Endogâmicos ICR
Estrutura Molecular
Fragmentos de Peptídeos/antagonistas & inibidores
Agregados Proteicos/efeitos dos fármacos
Hidrobrometo de Escopolamina
Relação Estrutura-Atividade
Tacrina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid beta-Peptides); 0 (Cholinesterase Inhibitors); 0 (Coumaric Acids); 0 (Ligands); 0 (Peptide Fragments); 0 (Protein Aggregates); 0 (amyloid beta-protein (1-42)); 451IFR0GXB (Scopolamine Hydrobromide); 4VX7YNB537 (Tacrine); AVM951ZWST (ferulic acid); EC 3.1.1.7 (Acetylcholinesterase); EC 3.1.1.8 (Butyrylcholinesterase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180207
[St] Status:MEDLINE
[do] DOI:10.1080/14756366.2018.1430691


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[PMID]:29278947
[Au] Autor:Chen Y; Zhu J; Mo J; Yang H; Jiang X; Lin H; Gu K; Pei Y; Wu L; Tan R; Hou J; Chen J; Lv Y; Bian Y; Sun H
[Ad] Endereço:a School of Pharmacy , Nanjing University of Chinese Medicine , Nanjing , China.
[Ti] Título:Synthesis and bioevaluation of new tacrine-cinnamic acid hybrids as cholinesterase inhibitors against Alzheimer's disease.
[So] Source:J Enzyme Inhib Med Chem;33(1):290-302, 2018 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Small molecule cholinesterases inhibitor (ChEI) provides an effective therapeutic strategy to treat Alzheimer's disease (AD). Currently, the discovery of new ChEI with multi-target effect is still of great importance. Herein, we report the synthesis, structure-activity relationship study and biological evaluation of a series of tacrine-cinnamic acid hybrids as new ChEIs. All target compounds are evaluated for their in vitro cholinesterase inhibitory activities. The representatives which show potent activity on cholinesterase, are evaluated for the amyloid ß-protein self-aggregation inhibition and in vivo assays. The optimal compound 19, 27, and 30 (human AChE IC = 10.2 ± 1.2, 16.5 ± 1.7, and 15.3 ± 1.8 nM, respectively) show good performance in ameliorating the scopolamine-induced cognition impairment and preliminary safety in hepatotoxicity evaluation. These compounds deserve further evaluation for the development of new therapeutic agents against AD.
[Mh] Termos MeSH primário: Doença de Alzheimer/tratamento farmacológico
Inibidores da Colinesterase/farmacologia
Cinamatos/farmacologia
Tacrina/farmacologia
[Mh] Termos MeSH secundário: Acetilcolinesterase/metabolismo
Doença de Alzheimer/metabolismo
Peptídeos beta-Amiloides/antagonistas & inibidores
Peptídeos beta-Amiloides/metabolismo
Animais
Butirilcolinesterase/metabolismo
Inibidores da Colinesterase/síntese química
Inibidores da Colinesterase/química
Cinamatos/química
Relação Dose-Resposta a Droga
Electrophorus
Cavalos
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos ICR
Modelos Moleculares
Estrutura Molecular
Agregados Proteicos/efeitos dos fármacos
Relação Estrutura-Atividade
Tacrina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid beta-Peptides); 0 (Cholinesterase Inhibitors); 0 (Cinnamates); 0 (Protein Aggregates); 4VX7YNB537 (Tacrine); EC 3.1.1.7 (Acetylcholinesterase); EC 3.1.1.8 (Butyrylcholinesterase); U14A832J8D (cinnamic acid)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171228
[St] Status:MEDLINE
[do] DOI:10.1080/14756366.2017.1412314


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[PMID]:28457693
[Au] Autor:Ahmad H; Ahmad S; Shah SAA; Latif A; Ali M; Khan FA; Tahir MN; Shaheen F; Wadood A; Ahmad M
[Ad] Endereço:Department of Chemistry, University of Malakand, Chakdara, Dir (L) 18550, KP, Pakistan.
[Ti] Título:Antioxidant and anticholinesterase potential of diterpenoid alkaloids from Aconitum heterophyllum.
[So] Source:Bioorg Med Chem;25(13):3368-3376, 2017 07 01.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Extensive chromatographic separations performed on the basic (pH=8-10) chloroform soluble fraction of Aconitum heterophyllum resulted in the isolation of three new diterpenoid alkaloids, 6ß-Methoxy, 9ß-dihydroxylheteratisine (1), 1α,11,13ß-trihydroxylhetisine (2), 6,15ß-dihydroxylhetisine (3), and the known compounds iso-atisine (4), heteratisine (5), hetisinone (6), 19-epi-isoatisine (7), and atidine (8). Structures of the isolated compounds were established by means of mass and NMR spectroscopy as well as single crystal X-ray crystallography. Compounds 1-8 were screened for their antioxidant and enzyme inhibition activities followed by in silico studies to find out the possible inhibitory mechanism of the tested compounds. This work is the first report demonstrating significant antioxidant and anticholinesterase potentials of diterpenoid alkaloids isolated from a natural source.
[Mh] Termos MeSH primário: Aconitum/química
Alcaloides/farmacologia
Antioxidantes/farmacologia
Inibidores da Colinesterase/farmacologia
Colinesterases/metabolismo
Diterpenos/farmacologia
[Mh] Termos MeSH secundário: Alcaloides/química
Alcaloides/isolamento & purificação
Animais
Antioxidantes/química
Antioxidantes/isolamento & purificação
Inibidores da Colinesterase/química
Inibidores da Colinesterase/isolamento & purificação
Cristalografia por Raios X
Diterpenos/química
Diterpenos/isolamento & purificação
Relação Dose-Resposta a Droga
Electrophorus
Modelos Moleculares
Estrutura Molecular
Teoria Quântica
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Alkaloids); 0 (Antioxidants); 0 (Cholinesterase Inhibitors); 0 (Diterpenes); EC 3.1.1.8 (Cholinesterases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171208
[Lr] Data última revisão:
171208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


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[PMID]:28454848
[Au] Autor:Yan J; Hu J; Liu A; He L; Li X; Wei H
[Ad] Endereço:School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, China.
[Ti] Título:Design, synthesis, and evaluation of multitarget-directed ligands against Alzheimer's disease based on the fusion of donepezil and curcumin.
[So] Source:Bioorg Med Chem;25(12):2946-2955, 2017 06 15.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:By fusing donepezil and curcumin, a novel series of compounds were obtained as multitarget-directed ligands against Alzheimer's disease. Among them, compound 11b displayed potent acetylcholinesterase (AChE) inhibition (IC =187nM) and the highest BuChE/AChE selectivity (66.3). Compound 11b also inhibited 45.3% Aß self-aggregation at 20µM and displayed remarkable antioxidant effects. The metal-chelating property of compound 11b was elucidated by determining the 1:1 stoichiometry for the 11b-Cu(II) complex. The excellent blood-brain barrier permeability of 11b also indicated the potential for the compound to penetrate the central nervous system.
[Mh] Termos MeSH primário: Doença de Alzheimer/tratamento farmacológico
Peptídeos beta-Amiloides/metabolismo
Inibidores da Colinesterase/farmacologia
Curcumina/farmacologia
Indanos/farmacologia
Fragmentos de Peptídeos/metabolismo
Piperidinas/farmacologia
Agregados Proteicos/efeitos dos fármacos
[Mh] Termos MeSH secundário: Acetilcolinesterase/metabolismo
Doença de Alzheimer/enzimologia
Doença de Alzheimer/metabolismo
Animais
Barreira Hematoencefálica/metabolismo
Inibidores da Colinesterase/química
Inibidores da Colinesterase/farmacocinética
Curcumina/análogos & derivados
Curcumina/farmacocinética
Desenho de Drogas
Electrophorus
Seres Humanos
Indanos/química
Indanos/farmacocinética
Ligantes
Simulação de Acoplamento Molecular
Terapia de Alvo Molecular
Piperidinas/química
Piperidinas/farmacocinética
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid beta-Peptides); 0 (Cholinesterase Inhibitors); 0 (Indans); 0 (Ligands); 0 (Peptide Fragments); 0 (Piperidines); 0 (Protein Aggregates); 0 (amyloid beta-protein (1-42)); 8SSC91326P (donepezil); EC 3.1.1.7 (Acetylcholinesterase); IT942ZTH98 (Curcumin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171208
[Lr] Data última revisão:
171208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE


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[PMID]:28802122
[Au] Autor:Wiemann J; Karasch J; Loesche A; Heller L; Brandt W; Csuk R
[Ad] Endereço:Martin-Luther University Halle-Wittenberg, Organic Chemistry, Kurt-Mothes Str. 2, D-06120 Halle (Saale), Germany.
[Ti] Título:Piperlongumine B and analogs are promising and selective inhibitors for acetylcholinesterase.
[So] Source:Eur J Med Chem;139:222-231, 2017 Oct 20.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Piperlongumine B (19), an alkaloid previously isolated from long pepper (Piper longum) has been synthesized for the first time in a short sequence and in good yield together with 19 analogs. Screening of these compounds in Ellman's assays showed several of them to be good inhibitors of acetylcholinesterase while being less active for butyrylcholinesterase. Activity of the compounds increased with the ring size of the heterocycle, and a maximum of activity was observed for an analog holding 12 methylene groups in the aliphatic side chain. These compounds may be regarded as promising candidates for the development of efficient inhibitors of acetylcholinesterase being useful for the treatment of Alzheimer's disease.
[Mh] Termos MeSH primário: Acetilcolinesterase/metabolismo
Inibidores da Colinesterase/farmacologia
Dioxolanos/farmacologia
[Mh] Termos MeSH secundário: Animais
Butirilcolinesterase/metabolismo
Inibidores da Colinesterase/síntese química
Inibidores da Colinesterase/química
Dioxolanos/síntese química
Dioxolanos/química
Relação Dose-Resposta a Droga
Electrophorus/metabolismo
Estrutura Molecular
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cholinesterase Inhibitors); 0 (Dioxolanes); EC 3.1.1.7 (Acetylcholinesterase); EC 3.1.1.8 (Butyrylcholinesterase); HN39MC8KIO (piperlonguminine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170813
[St] Status:MEDLINE


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[PMID]:28797788
[Au] Autor:Wiemann J; Loesche A; Csuk R
[Ad] Endereço:Martin-Luther-University Halle-Wittenberg, Organic Chemistry, Kurt-Mothes-Str. 2, D-06120 Halle (Saale), Germany.
[Ti] Título:Novel dehydroabietylamine derivatives as potent inhibitors of acetylcholinesterase.
[So] Source:Bioorg Chem;74:145-157, 2017 Oct.
[Is] ISSN:1090-2120
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nowadays, the inhibition of acetylcholinesterase is one of the main pharmacological strategies for the treatment of Alzheimer's disease. Therefore, a set of thirty-four derivatives of the diterpenoid dehydroabietylamine has been synthesized and screened in colorimetric Ellman's assays to determine their ability to inhibit the enzymes acetylcholinesterase (AChE, from electric eel) and butyrylcholinesterase (BChE, from equine serum). A systematic variation of the substitution of dehydroabietylamides enabled an approach to analogs showing a remarkable inhibition potency for AChE. Particularly N-benzoyldehydroabietylamines 11, 12 and 13 were excellent inhibitors for AChE, showing inhibition rates comparable to standard galantamine hydrobromide.
[Mh] Termos MeSH primário: Acetilcolinesterase/metabolismo
Inibidores da Colinesterase/farmacologia
Diterpenos Abietanos/farmacologia
[Mh] Termos MeSH secundário: Animais
Inibidores da Colinesterase/síntese química
Inibidores da Colinesterase/química
Diterpenos Abietanos/síntese química
Diterpenos Abietanos/química
Relação Dose-Resposta a Droga
Electrophorus
Conformação Molecular
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cholinesterase Inhibitors); 0 (Diterpenes, Abietane); 0 (dehydroabietylamine); EC 3.1.1.7 (Acetylcholinesterase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170812
[St] Status:MEDLINE



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