Base de dados : MEDLINE
Pesquisa : D08.811.277.352.100.170.250 [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]:29335209
[Au] Autor:Chierrito TPC; Pedersoli-Mantoani S; Roca C; Sebastian-Pérez V; Martínez-Gonzalez L; Pérez DI; Perez C; Canales A; Cañada FJ; Campillo NE; Carvalho I; Martinez A
[Ad] Endereço:Centro de Investigaciones Biologicas (CIB-CSIC), Ramiro de Maetzu 9, Madrid, Spain; School of Pharmaceutical Sciences of Ribeirão Preto, University of São Paulo, Avenida do Café, s/ n, 14040-903, Ribeirão Preto, SP, Brazil.
[Ti] Título:Chameleon-like behavior of indolylpiperidines in complex with cholinesterases targets: Potent butyrylcholinesterase inhibitors.
[So] Source:Eur J Med Chem;145:431-444, 2018 Feb 10.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Alzheimer's disease (AD) is the most common form of dementia worldwide with an increasing prevalence for the next years. The multifactorial nature of AD precludes the design of new drugs directed to a single target being probably one of the reasons for recent failures. Therefore, dual binding site acetylcholinesterase (AChE) inhibitors have been revealed as cognitive enhancers and ß-amyloid modulators offering an alternative in AD therapy field. Based on the dual ligands NP61 and donepezil, the present study reports the synthesis of a series of indolylpiperidines hybrids to optimize the NP61 structure preserving the indole nucleus, but replacing the tacrine moiety of NP61 by benzyl piperidine core found in donepezil. Surprisingly, this new family of indolylpiperidines derivatives showed very potent and selective hBuChE inhibition. Further studies of NMR and molecular dynamics have showed the capacity of these hybrid molecules to change their bioactive conformation depending on the binding site, being capable to inhibit with different shapes BuChE and residually AChE.
[Mh] Termos MeSH primário: Acetilcolinesterase/metabolismo
Butirilcolinesterase/metabolismo
Inibidores da Colinesterase/farmacologia
Indóis/farmacologia
Piperidinas/farmacologia
[Mh] Termos MeSH secundário: Inibidores da Colinesterase/síntese química
Inibidores da Colinesterase/química
Relação Dose-Resposta a Droga
Seres Humanos
Indóis/síntese química
Indóis/química
Estrutura Molecular
Piperidinas/síntese química
Piperidinas/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cholinesterase Inhibitors); 0 (Indoles); 0 (Indolylpiperidine); 0 (Piperidines); 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:180117
[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]:29447012
[Au] Autor:Gao X; Tang J; Liu H; Liu L; Kang L; Chen W
[Ad] Endereço:a Key Laboratory Breeding Base of Hu'nan Oriented Fundamental and Applied Research of Innovative Pharmaceutics, College of Pharmacy , Changsha Medical University , Changsha , China.
[Ti] Título:Structure-activity relationship investigation of tertiary amine derivatives of cinnamic acid as acetylcholinesterase and butyrylcholinesterase inhibitors: compared with that of phenylpropionic acid, sorbic acid and hexanoic acid.
[So] Source:J Enzyme Inhib Med Chem;33(1):519-524, 2018 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In the present investigation, 48 new tertiary amine derivatives of cinnamic acid, phenylpropionic acid, sorbic acid and hexanoic acid (4d-6g, 10d-12g, 16d-18g and 22d-24g) were designed, synthesized and evaluated for the effect on AChE and BChE in vitro. The results revealed that the alteration of aminoalkyl types and substituted positions markedly influences the effects in inhibiting AChE. Almost of all cinnamic acid derivatives had the most potent inhibitory activity than that of other acid derivatives with the same aminoalkyl side chain. Unsaturated bond and benzene ring in cinnamic acid scaffold seems important for the inhibitory activity against AChE. Among them, compound 6g revealed the most potent AChE inhibitory activity (IC value: 3.64 µmol/L) and highest selectivity over BChE (ratio: 28.6). Enzyme kinetic study showed that it present a mixed-type inhibition against AChE. The molecular docking study suggested that it can bind with the catalytic site and peripheral site of AChE.
[Mh] Termos MeSH primário: Aminas/farmacologia
Caproatos/farmacologia
Inibidores da Colinesterase/farmacologia
Cinamatos/farmacologia
Fenilpropionatos/farmacologia
Ácido Sórbico/farmacologia
[Mh] Termos MeSH secundário: Acetilcolinesterase/metabolismo
Aminas/síntese química
Aminas/química
Animais
Butirilcolinesterase/metabolismo
Caproatos/química
Inibidores da Colinesterase/síntese química
Inibidores da Colinesterase/química
Cinamatos/química
Relação Dose-Resposta a Droga
Simulação de Acoplamento Molecular
Estrutura Molecular
Fenilpropionatos/química
Ratos
Ratos Sprague-Dawley
Ácido Sórbico/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amines); 0 (Caproates); 0 (Cholinesterase Inhibitors); 0 (Cinnamates); 0 (Phenylpropionates); 1F8SN134MX (hexanoic acid); 5Q445IN5CU (3-phenylpropionic acid); EC 3.1.1.7 (Acetylcholinesterase); EC 3.1.1.8 (Butyrylcholinesterase); U14A832J8D (cinnamic acid); X045WJ989B (Sorbic Acid)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180219
[Lr] Data última revisão:
180219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180216
[St] Status:MEDLINE
[do] DOI:10.1080/14756366.2018.1436053


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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]:28463565
[Au] Autor:Ahmad H; Ahmad S; Shah SAA; Khan HU; Khan FA; Ali M; Latif A; Shaheen F; Ahmad M
[Ad] Endereço:a Department of Chemistry , University of Malakand , Dir (Lower) 18550 , Pakistan.
[Ti] Título:Selective dual cholinesterase inhibitors from Aconitum laeve.
[So] Source:J Asian Nat Prod Res;20(2):172-181, 2018 Feb.
[Is] ISSN:1477-2213
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:New lycoctonine-type dual cholinesterase inhibitor, swatinine-C (1), along with three known norditerpenoid alkaloids, hohenackerine (2), aconorine (5) and lappaconitine (6) and two synthetically known but phytochemically new benzene derivatives, methyl 2-acetamidobenzoate (3) and methyl 4-[2-(methoxycarbonyl)anilino]-4-oxobutanoate (4), was isolated from the roots of A. laeve. Structures of new and known compounds (1-6) were established on the basis of latest spectroscopic techniques and by close comparison with the data available in literature. In vitro, compounds (1-6) were tested against AChE and BChE inhibitory activities. Compounds 1 and 2 showed competitive inhibition against AChE (IC = 3.7 µM, 4.53 µM) and BChE (IC = 12.23 µM, 9.94 µM), respectively. Compounds 5 and 6 showed promising noncompetitive type of inhibitory profile against AChE (IC = 2.51 and 6.13 µM) only. Compounds 3 and 4 showed weak inhibitory profile against both AChE and BChE.
[Mh] Termos MeSH primário: Aconitum/química
Inibidores da Colinesterase/isolamento & purificação
Inibidores da Colinesterase/farmacologia
[Mh] Termos MeSH secundário: Aconitina/análogos & derivados
Aconitina/química
Aconitina/isolamento & purificação
Aconitina/farmacologia
Alcaloides/química
Alcaloides/isolamento & purificação
Butirilcolinesterase/metabolismo
Inibidores da Colinesterase/química
Estrutura Molecular
Raízes de Plantas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alkaloids); 0 (Cholinesterase Inhibitors); 0GLX1UNC80 (lycoctonine); EC 3.1.1.8 (Butyrylcholinesterase); X8YN71D5WC (Aconitine); Y4M5974F7Z (lappaconitine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1080/10286020.2017.1319820


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[PMID]:27770414
[Au] Autor:Johnson GR; Luckarift HR
[Ad] Endereço:Hexpoint Technologies, 503 Maryland Boulevard, Mexico Beach, FL, 32456, USA.
[Ti] Título:Enzyme Stabilization via Bio-Templated Silicification Reactions.
[So] Source:Methods Mol Biol;1504:61-73, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Effective entrapment of enzymes in solid phase materials is critical to their practical application. The entrapment generally stabilizes biological activity compared to soluble molecules and the material simplifies catalyst integration compared to other methods. A silica sol-gel process based upon biological mechanisms of inorganic material formation (biomineralization) supports protein immobilization reactions within minutes. The material has high protein binding capacity and the catalytic activity of the enzyme is retained. We have demonstrated that both oligopeptides and selected proteins will mediate the biomineralization of silica and allow effective co-encapsulation of other proteins present in the reaction mixture. The detailed methods described here provide a simple and effective approach for molecular biologists, biochemists and bioengineers to create stable, solid phase biocatalysts that may be integrated within sensors, synthetic processes, reactive barriers, energy conversion, and other biotechnology concepts.
[Mh] Termos MeSH primário: Butirilcolinesterase/química
Enzimas Imobilizadas/química
Muramidase/química
Dióxido de Silício/química
[Mh] Termos MeSH secundário: Animais
Técnicas Biossensoriais
Biotecnologia
Butirilcolinesterase/metabolismo
Galinhas
Ensaios Enzimáticos/métodos
Enzimas Imobilizadas/metabolismo
Muramidase/metabolismo
Peptídeos/química
Transição de Fase
Sílica Gel/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Peptides); 60650-90-0 (Silica Gel); 7631-86-9 (Silicon Dioxide); EC 3.1.1.8 (Butyrylcholinesterase); EC 3.2.1.17 (Muramidase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180115
[Lr] Data última revisão:
180115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE


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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]:29190644
[Au] Autor:Bernardi A; Kirschner KN; Faller R
[Ad] Endereço:Department of Chemical Engineering, University of California-Davis, Davis, California, United States of America.
[Ti] Título:Structural analysis of human glycoprotein butyrylcholinesterase using atomistic molecular dynamics: The importance of glycosylation site ASN241.
[So] Source:PLoS One;12(11):e0187994, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human butyrylcholinesterase (BChE) is a glycoprotein capable of bioscavenging toxic compounds such as organophosphorus (OP) nerve agents. For commercial production of BChE, it is practical to synthesize BChE in non-human expression systems, such as plants or animals. However, the glycosylation profile in these systems is significantly different from the human glycosylation profile, which could result in changes in BChE's structure and function. From our investigation, we found that the glycan attached to ASN241 is both structurally and functionally important due to its close proximity to the BChE tetramerization domain and the active site gorge. To investigate the effects of populating glycosylation site ASN241, monomeric human BChE glycoforms were simulated with and without site ASN241 glycosylated. Our simulations indicate that the structure and function of human BChE are significantly affected by the absence of glycan 241.
[Mh] Termos MeSH primário: Butirilcolinesterase/química
[Mh] Termos MeSH secundário: Glicosilação
Seres Humanos
Simulação de Dinâmica Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.1.1.8 (Butyrylcholinesterase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0187994


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[PMID]:29210299
[Au] Autor:Czarnecka K; Girek M; Maciejewska K; Skibinski R; Jonczyk J; Bajda M; Kabzinski J; Solowiej P; Majsterek I; Szymanski P
[Ad] Endereço:a Department of Pharmaceutical Chemistry, Drug Analyses and Radiopharmacy, Faculty of Pharmacy , Medical University of Lodz , Lodz , Poland.
[Ti] Título:New cyclopentaquinoline hybrids with multifunctional capacities for the treatment of Alzheimer's disease.
[So] Source:J Enzyme Inhib Med Chem;33(1):158-170, 2017 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Alzheimer's disease (AD) is the most common progressive form of brain neurodegeneration and the most prevailing cause of dementia. Unfortunately, the aetiology of AD is not completely studied but different factors are associated with the development of AD such as among others low level of acetylcholine, aggregation of ß-amyloid (Aß), hyperphosphorylated tau protein, oxidative stress, and inflammation. The study encompass organic syntheses of 2,3-dihydro-1H-cyclopenta[b]quinoline with 5,6-dichloronicotinic acid and suitable linkers derivatives as multifunctional agents for AD treatment. Afterwards self-induced amyloid beta aggregation, inhibition studies of acetylcholinesterase and butyrylcholinesterase and molecular docking studies were performed. The results showed that 3b compound exhibited the best acetylcholinesterase inhibitory activity, with IC value of 0.052 µM which is lower compared to references. Besides, all synthesised compounds showed good butyrylcholinesterase inhibitory activity with IC values from 0.071 to 0.797 µM. Compound 3b exhibited strong Aß aggregation inhibitory effect with 25.7% at 5 µM to 92.8% at 100 µM as well as good anti-inflammatory effect. Thus, new compounds could create new perspectives for further development as a multi-target-directed agent for AD treatment.
[Mh] Termos MeSH primário: Acetilcolinesterase/metabolismo
Doença de Alzheimer/tratamento farmacológico
Aminoquinolinas/farmacologia
Butirilcolinesterase/metabolismo
Inibidores da Colinesterase/farmacologia
Inibidores de Glicosídeo Hidrolases/farmacologia
Hialuronoglucosaminidase/antagonistas & inibidores
Niacinamida/análogos & derivados
[Mh] Termos MeSH secundário: Doença de Alzheimer/metabolismo
Aminoquinolinas/síntese química
Aminoquinolinas/química
Peptídeos beta-Amiloides/antagonistas & inibidores
Peptídeos beta-Amiloides/metabolismo
Animais
Proliferação Celular/efeitos dos fármacos
Inibidores da Colinesterase/síntese química
Inibidores da Colinesterase/química
Relação Dose-Resposta a Droga
Enguias
Inibidores de Glicosídeo Hidrolases/síntese química
Inibidores de Glicosídeo Hidrolases/química
Cavalos
Seres Humanos
Hialuronoglucosaminidase/metabolismo
Modelos Moleculares
Estrutura Molecular
Niacinamida/síntese química
Niacinamida/química
Niacinamida/farmacologia
Fragmentos de Peptídeos/antagonistas & inibidores
Fragmentos de Peptídeos/metabolismo
Agregados Proteicos/efeitos dos fármacos
Relação Estrutura-Atividade
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5,6-dichloro-N-(3-(2,3-dihydro-1H-cyclopenta(b)quinolin-9-ylamino)propyl)nicotinamide); 0 (Aminoquinolines); 0 (Amyloid beta-Peptides); 0 (Cholinesterase Inhibitors); 0 (Glycoside Hydrolase Inhibitors); 0 (Peptide Fragments); 0 (Protein Aggregates); 0 (amyloid beta-protein (1-42)); 25X51I8RD4 (Niacinamide); EC 3.1.1.7 (Acetylcholinesterase); EC 3.1.1.8 (Butyrylcholinesterase); EC 3.2.1.35 (Hyaluronoglucosaminidase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE
[do] DOI:10.1080/14756366.2017.1406485



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