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  1 / 215 MEDLINE  
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[PMID]:22850215
[Au] Autor:Kunciw DL; Liechty JJ; Mitchell MO; Wan B; Franzblau SG
[Ad] Endereço:Department of Chemistry, Salisbury University, Salisbury, MD 21801, USA.
[Ti] Título:Structural requirements for the antitubercular quaternized triflupromazine pharmacophore.
[So] Source:Bioorg Med Chem Lett;22(17):5679-80, 2012 Sep 01.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Quaternized triflupromazine derivatives (QTDs) must possess benzyl groups attached to the quaternary nitrogen in order to have significant antitubercular potency. Replacing the quaternary amine with a triazole abolishes antitubercular activity. A modest halogen substitution effect exists, with the 4-bromophenyl QTD 3 having the best selectivity index (>21). All N-benzyl QTDs 1-4 similarly inhibit non-replicating, persistent Mycobacterium tuberculosis with MIC<8 µM, and compounds 1-3 were all nontoxic to mammalian cells in vitro (IC(50)>128 µM).
[Mh] Termos MeSH primário: Antituberculosos/química
Antituberculosos/farmacologia
Mycobacterium tuberculosis/efeitos dos fármacos
Triflupromazina/análogos & derivados
Triflupromazina/farmacologia
[Mh] Termos MeSH secundário: Animais
Sobrevivência Celular/efeitos dos fármacos
Cercopithecus aethiops
Seres Humanos
Testes de Sensibilidade Microbiana
Relação Estrutura-Atividade
Tuberculose/tratamento farmacológico
Células Vero
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antitubercular Agents); RO16TQF95Y (Triflupromazine)
[Em] Mês de entrada:1301
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120802
[St] Status:MEDLINE
[do] DOI:10.1016/j.bmcl.2012.06.095


  2 / 215 MEDLINE  
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[PMID]:20060828
[Au] Autor:Taft AS; Norante FA; Yoshino TP
[Ad] Endereço:Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin, Madison, WI 53706, USA. tafta@svm.vetmed.wisc.edu
[Ti] Título:The identification of inhibitors of Schistosoma mansoni miracidial transformation by incorporating a medium-throughput small-molecule screen.
[So] Source:Exp Parasitol;125(2):84-94, 2010 Jun.
[Is] ISSN:1090-2449
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In Schistosoma mansoni, the miracidium-to-primary sporocyst transformation process is associated with many physiological, morphological, transcriptional and biochemical changes. In the present study, we use a medium-throughput small-molecule screen to identify chemical compounds inhibiting or delaying the in vitro transformation of miracidia to the sporocyst stage. The Sigma-Aldrich Library of Pharmacologically Active Compounds (LOPAC) contains 1280 well-characterized chemical compounds with various modes of action including enzyme inhibitors, antibiotics, cell-cycle regulators, apoptosis inducers and GPCR ligands. We identified 47 compounds that greatly reduce or delay this transformation process during a primary screen of live miracidia. The majority of compounds inhibiting larval transformation were from dopaminergic, serotonergic, ion channel and phosphorylation classes. Specifically, we found that dopamine D2-type antagonists, serotonin reuptake inhibitors, voltage-gated calcium channel antagonists and a PKC activator significantly reduced in vitro miracidial transformation rates. Many of the targets of these compounds regulate adenylyl cyclase activity, with the inhibition or activation of these targets resulting in increased cAMP levels in miracidia and concomitant blocking/delaying of larval transformation.
[Mh] Termos MeSH primário: Anti-Helmínticos/farmacologia
Schistosoma mansoni/efeitos dos fármacos
[Mh] Termos MeSH secundário: 1-Metil-3-Isobutilxantina/farmacologia
Animais
Benzofenantridinas/farmacologia
Calcimicina/farmacologia
Bloqueadores dos Canais de Cálcio/farmacologia
Citalopram/farmacologia
Clomipramina/farmacologia
Colforsina/farmacologia
AMP Cíclico/metabolismo
Dimetil Sulfóxido
Relação Dose-Resposta a Droga
Avaliação Pré-Clínica de Medicamentos/métodos
Imuno-Histoquímica
Camundongos
Schistosoma mansoni/crescimento & desenvolvimento
Acetato de Tetradecanoilforbol/farmacologia
Triflupromazina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Anthelmintics); 0 (Benzophenanthridines); 0 (Calcium Channel Blockers); 0DHU5B8D6V (Citalopram); 1F7A44V6OU (Colforsin); 37H9VM9WZL (Calcimycin); E0399OZS9N (Cyclic AMP); E3B045W6X0 (chelerythrine); NI40JAQ945 (Tetradecanoylphorbol Acetate); NUV44L116D (Clomipramine); RO16TQF95Y (Triflupromazine); TBT296U68M (1-Methyl-3-isobutylxanthine); YOW8V9698H (Dimethyl Sulfoxide)
[Em] Mês de entrada:1005
[Cu] Atualização por classe:170930
[Lr] Data última revisão:
170930
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100112
[St] Status:MEDLINE
[do] DOI:10.1016/j.exppara.2009.12.021


  3 / 215 MEDLINE  
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[PMID]:19713760
[Au] Autor:Riffell JL; Zimmerman C; Khong A; McHardy LM; Roberge M
[Ad] Endereço:Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada.
[Ti] Título:Effects of chemical manipulation of mitotic arrest and slippage on cancer cell survival and proliferation.
[So] Source:Cell Cycle;8(18):3025-38, 2009 Sep 15.
[Is] ISSN:1551-4005
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Microtubule-targeting cancer therapies interfere with mitotic spindle dynamics and block cells in mitosis by activating the mitotic checkpoint. Cells arrested in mitosis may remain arrested for extended periods of time or undergo mitotic slippage and enter interphase without having separated their chromosomes. How extended mitotic arrest and mitotic slippage contribute to subsequent cell death or survival is incompletely understood. To address this question, automated fluorescence microscopy assays were designed and used to screen chemical libraries for modulators of mitotic slippage. Chlorpromazine and triflupromazine were identified as drugs that inhibit mitotic slippage and SU6656 and geraldol as chemicals that stimulate mitotic slippage. Using the drugs to extend mitotic arrest imposed by low concentrations of paclitaxel led to increased cell survival and proliferation after drug removal. Cells arrested at mitosis with paclitaxel or vinblastine and chemically induced to undergo mitotic slippage underwent several rounds of DNA replication without cell division and exhibited signs of senescence but eventually all died. By contrast, cells arrested at mitosis with the KSP/Eg5 inhibitor S-trityl-L-cysteine and induced to undergo mitotic slippage were able to successfully divide and continued to proliferate after drug removal. These results show that reinforcing mitotic arrest with drugs that inhibit mitotic slippage can lead to increased cell survival and proliferation, while inducing mitotic slippage in cells treated with microtubule-targeting drugs seems to lead to protracted cell death.
[Mh] Termos MeSH primário: Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Flavonas/farmacologia
Mitose/efeitos dos fármacos
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Clorpromazina/farmacologia
Cisteína/análogos & derivados
Cisteína/farmacologia
Seres Humanos
Indóis/farmacologia
Microtúbulos/efeitos dos fármacos
Paclitaxel/farmacologia
Sulfonamidas/farmacologia
Triflupromazina/farmacologia
Vimblastina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (3,4',7-trihydroxy-3'-methoxyflavone); 0 (Flavones); 0 (Indoles); 0 (SU 6656); 0 (Sulfonamides); 2799-07-7 (3-tritylthio-L-alanine); 5V9KLZ54CY (Vinblastine); K848JZ4886 (Cysteine); P88XT4IS4D (Paclitaxel); RO16TQF95Y (Triflupromazine); U42B7VYA4P (Chlorpromazine)
[Em] Mês de entrada:0912
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090829
[St] Status:MEDLINE


  4 / 215 MEDLINE  
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[PMID]:19461075
[Au] Autor:Chen CL; Hou WH; Liu IH; Hsiao G; Huang SS; Huang JS
[Ad] Endereço:Department of Biochemistry, Saint Louis University School of Medicine, Doisy Research Center, St Louis, MO 63104, USA.
[Ti] Título:Inhibitors of clathrin-dependent endocytosis enhance TGFbeta signaling and responses.
[So] Source:J Cell Sci;122(Pt 11):1863-71, 2009 Jun 01.
[Is] ISSN:0021-9533
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Clathrin-dependent endocytosis is believed to be involved in TGFbeta-stimulated cellular responses, but the subcellular locus at which TGFbeta induces signaling remains unclear. Here, we demonstrate that inhibitors of clathrin-dependent endocytosis, which are known to arrest the progression of endocytosis at coated-pit stages, inhibit internalization of cell-surface-bound TGFbeta and promote colocalization and accumulation of TbetaR-I and SARA at the plasma membrane. These inhibitors enhance TGFbeta-induced signaling and cellular responses (Smad2 phosphorylation/nuclear localization and expression of PAI-1). Dynasore, a newly identified inhibitor of dynamin GTPase activity, is one of the most potent inhibitors among those tested and, furthermore, is a potent enhancer of TGFbeta. Dynasore ameliorates atherosclerosis in the aortic endothelium of hypercholesterolemic ApoE-null mice by counteracting the suppressed TGFbeta responsiveness caused by the hypercholesterolemia, presumably acting through its effect on TGFbeta endocytosis and signaling in vascular cells.
[Mh] Termos MeSH primário: Clatrina/metabolismo
Endocitose/fisiologia
Transdução de Sinais/fisiologia
Fator de Crescimento Transformador beta/metabolismo
[Mh] Termos MeSH secundário: Animais
Apolipoproteínas E/genética
Apolipoproteínas E/metabolismo
Cadaverina/análogos & derivados
Cadaverina/farmacologia
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Linhagem Celular
Endocitose/efeitos dos fármacos
Inibidores Enzimáticos/farmacologia
Feminino
Hidrazonas/farmacologia
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Monensin/farmacologia
Inibidor 1 de Ativador de Plasminogênio/genética
Inibidor 1 de Ativador de Plasminogênio/metabolismo
Proteínas Serina-Treonina Quinases/genética
Proteínas Serina-Treonina Quinases/metabolismo
Receptores de Fatores de Crescimento Transformadores beta/genética
Receptores de Fatores de Crescimento Transformadores beta/metabolismo
Transdução de Sinais/efeitos dos fármacos
Proteína Smad2/metabolismo
Triflupromazina/farmacologia
beta-Ciclodextrinas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Apolipoproteins E); 0 (Carrier Proteins); 0 (Clathrin); 0 (Enzyme Inhibitors); 0 (Hydrazones); 0 (N'-(3,4-dihydroxybenzylidene)-3-hydroxy-2-naphthahydrazide); 0 (Plasminogen Activator Inhibitor 1); 0 (Receptors, Transforming Growth Factor beta); 0 (SARA protein, mouse); 0 (Smad2 Protein); 0 (Smad2 protein, mouse); 0 (Transforming Growth Factor beta); 0 (beta-Cyclodextrins); 906O0YJ6ZP (Monensin); EC 2.7.1.11 (TGF-beta type I receptor); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); I9N81SC5HD (monodansylcadaverine); JV039JZZ3A (betadex); L90BEN6OLL (Cadaverine); RO16TQF95Y (Triflupromazine)
[Em] Mês de entrada:0909
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090523
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.038729


  5 / 215 MEDLINE  
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[PMID]:19282733
[Au] Autor:Akel I; Kocak O; Bozkurt G; Alanay A; Marcucio R; Acaroglu E
[Ad] Endereço:Department of Orthopedics and Traumatology, Hacettepe University, Ankara, Turkey.
[Ti] Título:The effect of calmodulin antagonists on experimental scoliosis: a pinealectomized chicken model.
[So] Source:Spine (Phila Pa 1976);34(6):533-8, 2009 Mar 15.
[Is] ISSN:1528-1159
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:STUDY DESIGN: Randomized controlled. OBJECTIVE: To evaluate the effects of Tamoxifen (TMX) and trifluoperozine (TFP) on pinealectomized chicken scoliosis. SUMMARY OF BACKGROUND DATA: Pinealectomized chicken develops scoliosis probably due to the lack of melatonin. In addition to other functions, melatonin also acts as a calmodulin antagonist. We postulate that loss of this antagonistic effect may be the cause of scoliosis in this model. TMX and TFP are known calmodulin antagonists, which may alter the incidence and severity of scoliosis. METHODS: Seventy-two newly hatched chicken that underwent surgical pinealectomy within 72 hours of hatching were divided into 3 groups of 24 animals in each as group I (control), group II (TMX), and group III (TFP). TMX and TFP were given to groups II and III, respectively, for 10 weeks with the dose of 0.1 mg/kg/d, whereas the control group received no medication. AP scoliosis radiographs were obtained at seventh and 10th week to evaluate coronal spinal alignment. RESULTS: Three chickens in group I, 2 chickens in group II, and 1 chicken in group III died in the first postoperative week. Scoliosis incidences and magnitudes were similar among groups at seventh and 10th week. TMX and TFP groups showed decreases of incidence of upper cervical, lower cervical, lower cervical-thoracic-lumbar curves at 10th week compared with seventh week. TMX group showed a decline in thoracic region mean Cobb angle, whereas control group showed an increase (P = 0.048). TMX group showed a more prominent decline in cervicothoracic region mean Cobb angle compared with control group (P = 0.009). CONCLUSION: The incidence and magnitude of scoliosis in pinealectomized chicken may be decreased by the administration of TMX, presumably because of this drugs' calmodulin antagonism. Further studies on higher animals and dosage and timing are required.
[Mh] Termos MeSH primário: Calmodulina/antagonistas & inibidores
Glândula Pineal/cirurgia
Escoliose/tratamento farmacológico
Tamoxifeno/farmacologia
Triflupromazina/farmacologia
[Mh] Termos MeSH secundário: Animais
Conservadores da Densidade Óssea/farmacologia
Calmodulina/metabolismo
Galinhas
Modelos Animais de Doenças
Antagonistas de Dopamina/farmacologia
Feminino
Melatonina/deficiência
Glândula Pineal/metabolismo
Radiografia
Escoliose/diagnóstico por imagem
Escoliose/etiologia
Índice de Gravidade de Doença
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bone Density Conservation Agents); 0 (Calmodulin); 0 (Dopamine Antagonists); 094ZI81Y45 (Tamoxifen); JL5DK93RCL (Melatonin); RO16TQF95Y (Triflupromazine)
[Em] Mês de entrada:0905
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090314
[St] Status:MEDLINE
[do] DOI:10.1097/BRS.0b013e31818be0b1


  6 / 215 MEDLINE  
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[PMID]:18675773
[Au] Autor:Kim MJ; Pal S; Naoghare PK; Song JM
[Ad] Endereço:Research Institute of Pharmaceutical Sciences and College of Pharmacy, Seoul National University, 599 Gwanangno, Gwanak-gu, Seoul, Republic of Korea.
[Ti] Título:Monitoring the (photo)genotoxicity of photosensitizer drugs: direct quantitation of single-strand breaks in deoxyribonucleic acid using an oligonucleotide chip.
[So] Source:Anal Biochem;382(1):40-7, 2008 Nov 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Oligonucleotide chip-based assays can be a sample-thrifty, time-saving, routine tool for evaluation of chemical-induced DNA strand breaks. This article describes a novel approach using an oligonucleotide chip to determine photosensitizer-induced DNA single-strand breaks. Surface coverage of fluorophore-labeled oligonucleotides on silicon dioxide chip surfaces was determined on alkaline phosphatase digestion. Fluorescence maxima (at 520 nm) of the solutions were converted to molar concentrations of the fluorescein-modified oligonucleotide by interpolation from a predetermined standard linear calibration curve. The photosensitizing activity of chlorpromazine and triflupromazine toward DNA single-strand breaks was then studied at different drug doses and also as a function of photoirradiation time. Photoinduced single-strand breaks calculated using the method described here agreed with values predicted by theoretical extrapolation of the single-strand breaks obtained for plasmid DNAs from agarose gel electrophoresis, and thereby indirectly validated the chip-based assays. Under UV irradiation (>or=93.6 kJ/m2) chlorpromazine (>or=0.08 mM) was found to have significant photogenotoxicity. However, triflupromazine did not exhibit any (photo)genotoxicity over the concentration range studied (0.04-0.20mM). The method developed will be useful for quantitative screening of drug genotoxicity in terms of induction of breaks in DNA.
[Mh] Termos MeSH primário: Quebras de DNA de Cadeia Simples/efeitos dos fármacos
DNA/metabolismo
Mutagênicos/toxicidade
Análise de Sequência com Séries de Oligonucleotídeos
Fármacos Fotossensibilizantes/toxicidade
[Mh] Termos MeSH secundário: Sequência de Bases
Clorpromazina/toxicidade
DNA/genética
Quebras de DNA de Cadeia Simples/efeitos da radiação
Relação Dose-Resposta a Droga
Relação Dose-Resposta à Radiação
Propriedades de Superfície
Fatores de Tempo
Triflupromazina/toxicidade
Raios Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Mutagens); 0 (Photosensitizing Agents); 9007-49-2 (DNA); RO16TQF95Y (Triflupromazine); U42B7VYA4P (Chlorpromazine)
[Em] Mês de entrada:0901
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080805
[St] Status:MEDLINE
[do] DOI:10.1016/j.ab.2008.07.015


  7 / 215 MEDLINE  
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[PMID]:18020438
[Au] Autor:Cheema MA; Taboada P; Barbosa S; Castro E; Siddiq M; Mosquera V
[Ad] Endereço:Grupo de Física de Coloides y Polímeros, Departamento de Física de la Materia Condensada, Facultad de Física, Universidad de Santiago de Compostela, E-15782, Santiago de Compostela, Spain.
[Ti] Título:Modification of the thermal unfolding pathways of myoglobin upon drug interaction in different aqueous media.
[So] Source:J Phys Chem B;111(49):13851-7, 2007 Dec 13.
[Is] ISSN:1520-6106
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this work, we have analyzed the influence of two structurally related phenothiazine drugs, promazine and triflupromazine hydrochlorides, when bound to myoglobin, a model protein, and how the drug concentration and solution conditions may affect the denaturation process of this protein. In this manner, we derive the thermodynamic quantities of the unfolding process by using a spectroscopic technique such as UV-vis spectroscopy at different drugs concentrations and at pH 2.5, 5.5, and 9.0. To do this, a thermodynamic model was used which included experimental data corresponding to the pre- and post-transition into the observable transition. It has been found that both drugs play a destabilizing role for the protein, at least at low concentrations. In addition, at acidic pH and higher drug concentrations, a stabilizing effect can be observed, which may be related to the formation of some type of protein refolding, subsequent aggregation, or both. The reason for this behavior has been suggested to be the different protein conformations at acidic pH, the increase of solvent-exposed hydrophobic and hydrophilic residues after denaturation and/or binding, and the different strength of drug-protein interactions when changing the solution conditions. For this reason, thermodynamic quantities such as Gibbs energies, DeltaG, and entropies of unfolding, DeltaS(m), increase as the solution pH increases provided that additional solvent-exposed hydrophobic residues are present, which were previously buried at room temperature. Moreover, the larger binding affinity at pH 9.0 due to enhanced electrostatic interactions between protein and drug molecules (drug and protein differ in their net electrical charge) additionally collaborates to this residue exposition to solvent as a consequence of the alteration of protein conformation as due to drug binding. Comparison of thermodynamic data between promazine and triflupromazine hydrochlorides also shows that drug-protein affinity and hydrophobicity also affect the thermodynamic denaturation parameters.
[Mh] Termos MeSH primário: Mioglobina/química
Promazina/química
Triflupromazina/química
[Mh] Termos MeSH secundário: Animais
Cavalos
Desnaturação Proteica
Espectrofotometria Ultravioleta
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Myoglobin); O9M39HTM5W (Promazine); RO16TQF95Y (Triflupromazine)
[Em] Mês de entrada:0804
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:071121
[St] Status:MEDLINE


  8 / 215 MEDLINE  
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[PMID]:17188865
[Au] Autor:Bate AB; Kalin JH; Fooksman EM; Amorose EL; Price CM; Williams HM; Rodig MJ; Mitchell MO; Cho SH; Wang Y; Franzblau SG
[Ad] Endereço:Department of Chemistry, Salisbury University, Salisbury, MD 21801, USA.
[Ti] Título:Synthesis and antitubercular activity of quaternized promazine and promethazine derivatives.
[So] Source:Bioorg Med Chem Lett;17(5):1346-8, 2007 Mar 01.
[Is] ISSN:0960-894X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Quaternized chlorpromazine, triflupromazine, and promethazine derivatives were synthesized and examined as antitubercular agents against both actively growing and non-replicating Mycobacterium tuberculosis H37Rv. Impressively, several compounds inhibited non-replicating M. tuberculosis at concentrations equal to or double their MICs against the actively growing strain. All active compounds were non-toxic toward Vero cells (IC50 > 128 microM). N-Allylchlorpromazinium bromide was only weakly antitubercular, but replacing allyl with benzyl or substituted benzyl improved potency. An electron-withdrawing substituent on the phenothiazine ring was also essential. Branching at the carbon chain decreased antitubercular activity. The optimum antitubercular structures possessed N-(4- or 3-chlorobenzyl) substitution on triflupromazine.
[Mh] Termos MeSH primário: Antituberculosos/síntese química
Antituberculosos/farmacologia
[Mh] Termos MeSH secundário: Clorpromazina/síntese química
Clorpromazina/farmacologia
Mycobacterium tuberculosis/efeitos dos fármacos
Promazina/síntese química
Promazina/farmacologia
Prometazina/síntese química
Prometazina/farmacologia
Compostos de Amônio Quaternário/síntese química
Compostos de Amônio Quaternário/farmacologia
Relação Estrutura-Atividade
Triflupromazina/síntese química
Triflupromazina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antitubercular Agents); 0 (Quaternary Ammonium Compounds); FF28EJQ494 (Promethazine); O9M39HTM5W (Promazine); RO16TQF95Y (Triflupromazine); U42B7VYA4P (Chlorpromazine)
[Em] Mês de entrada:0705
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:061226
[St] Status:MEDLINE


  9 / 215 MEDLINE  
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[PMID]:16819214
[Au] Autor:Kitamura K; Omran AA; Nagata C; Kamijima Y; Tanaka R; Takegami S; Kitade T
[Ad] Endereço:Kyoto Pharmaceutical University; 5 Nakauchicho, Yamashina-ku, Kyoto 607-8414, Japan. kitamura@mb.kyoto-phu.ac.jp
[Ti] Título:Effects of inorganic ions on the binding of triflupromazine and chlorpromazine to bovine serum albumin studied by spectrometric methods.
[So] Source:Chem Pharm Bull (Tokyo);54(7):972-6, 2006 Jul.
[Is] ISSN:0009-2363
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:The effects of inorganic salts, NaCl, NaBr, NaI, Na2SO4, KCl, KBr, KI, on the binding constants (Ks) of psychotropic phenothiazine drugs, triflupromazine (TFZ) and chlorpromazine, to bovine serum albumin (BSA) were examined by using second-derivative spectrophotometry. All of the salts examined, with the exception of Na2SO4, decreased the K values significantly, depending on the concentration of the salt, e.g., the decrease in the K values of both drugs were about 40% for 0.1 M NaCl. The results obtained with Na2SO4 indicated that neither Na+ nor SO4(2-) had any affect on the binding of the phenothiazines to BSA. Based on the Na2SO4 results and the finding that the effect of each potassium salt on binding was quite similar to that of the corresponding sodium salt, the effects of these halogen salts can be considered to be derived from their anions, although the phenothiazines are positively charged at pH 7.4. The effectiveness of the anions was determined to occur in the following order: I->>Br->Cl-; these results coincided with the published order of the binding affinity of these anions to albumin. The 19F-NMR spectra of TFZ in the presence of each of these halogen salts revealed a concentration-dependent decrease in the intensity of the signal at 13.8 ppm that had previously been assigned to the TFZ bound to Site II. Consequently, the effects of these anions on the binding of positively charged phenothiazine drugs are thought to be local steric effects caused by the binding of these anions to Site II.
[Mh] Termos MeSH primário: Antipsicóticos/química
Clorpromazina/química
Ligação Proteica
Sais/química
Soroalbumina Bovina/química
Triflupromazina/química
[Mh] Termos MeSH secundário: Dicroísmo Circular
Íons/química
Íons/farmacologia
Espectroscopia de Ressonância Magnética
Ligação Proteica/efeitos dos fármacos
Sais/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antipsychotic Agents); 0 (Ions); 0 (Salts); 27432CM55Q (Serum Albumin, Bovine); RO16TQF95Y (Triflupromazine); U42B7VYA4P (Chlorpromazine)
[Em] Mês de entrada:0609
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:060705
[St] Status:MEDLINE


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[PMID]:15635254
[Au] Autor:Takegami S; Kitamura K; Kitade T; Takashima M; Ito M; Nakagawa E; Sone M; Sumitani R; Yasuda Y
[Ad] Endereço:Kyoto Pharmaceutical University, Kyoto, Japan.
[Ti] Título:Effects of phosphatidylserine and phosphatidylethanolamine content on partitioning of triflupromazine and chlorpromazine between phosphatidylcholine-aminophospholipid bilayer vesicles and water studied by second-derivative spectrophotometry.
[So] Source:Chem Pharm Bull (Tokyo);53(1):147-50, 2005 Jan.
[Is] ISSN:0009-2363
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:To assess the affinity of psychotropic phenothiazine drugs, triflupromazine (TFZ) and chlorpromazine (CPZ), for the membranes of central nervous system and the other organs in the body, the partition coefficients (Kps) of these drugs to phosphatidylcholine (PC)-phosphatidylserine (PS) and PC-phosphatidylethanolamine (PE) small and large unilamellar vesicles (SUV, LUV) were examined by a second-derivative spectrophotometric method, since PS is abundantly contained in the membranes of the central nervous system and PE is distributed widely in the membranes of the organs in the body. Size and preparation methods of the vesicles did not affect the Kp values at each aminophospholipid content suggesting that the partition of the phenothiazine drugs was not affected by the structural differences in the vesicles such as their curvature or asymmetric distribution of the phospholipids between the outer and inner layers of the bilayer membranes. However, the Kp values of both drugs increased remarkably according to the PS content in the bilayer membranes, i.e., the Kp values for the vesicles of 30 mol% PS content were about 3 times of that for the vesicles of PC alone, while both Kp values slightly reduced with the increase in the content of PE in the bilayer membranes of PC-PE vesicles. The results indicate that both drugs have higher affinity for the PC-PS bilayer membranes than for the PC and PC-PE membranes, which can offer an evidence for the fact that TFZ and CPZ are predominantly distributed and accumulated in the brain and nerve cell membranes that contain PS abundantly.
[Mh] Termos MeSH primário: Clorpromazina/análise
Glicerofosfolipídeos/análise
Bicamadas Lipídicas/análise
Triflupromazina/análise
[Mh] Termos MeSH secundário: Clorpromazina/química
Glicerofosfolipídeos/química
Bicamadas Lipídicas/química
Fosfatidilcolinas/análise
Fosfatidilcolinas/química
Fosfatidiletanolaminas/análise
Fosfatidiletanolaminas/química
Fosfatidilserinas/análise
Fosfatidilserinas/química
Espectrofotometria/métodos
Triflupromazina/química
Água/análise
Água/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycerophospholipids); 0 (Lipid Bilayers); 0 (Phosphatidylcholines); 0 (Phosphatidylethanolamines); 0 (Phosphatidylserines); 059QF0KO0R (Water); RO16TQF95Y (Triflupromazine); U42B7VYA4P (Chlorpromazine)
[Em] Mês de entrada:0505
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:050107
[St] Status:MEDLINE



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