Search results for "Structure–activity relationship"

showing 10 items of 290 documents

Synthesis and Biological Properties of Benzothiazole, Benzoxazole, and Chromen-4-one Analogues of the Potent Antitumor Agent 2-(3,4-Dimethoxyphenyl)-…

2008

New fluorinated 2-aryl-benzothiazoles, -benzoxazoles, and -chromen-4-ones have been synthesized and their activity against MCF-7 and MDA 468 breast cancer cell lines compared with the potent antitumor benzothiazole 5. Analogues such as 9a, b and 12a, d yielded submicromolar GI50 values in both cell lines; however, none of the new compounds approached 5 in terms of antitumor potency. For 5, binding to the aryl hydrocarbon receptor appeared to be necessary but not sufficient for growth inhibition.

BenzoxazolesBicyclic moleculebiologyStereochemistryCell CycleAntineoplastic AgentsBreast NeoplasmsBenzoxazoleAryl hydrocarbon receptorChemical synthesisIn vitroStructure-Activity Relationshipchemistry.chemical_compoundReceptors Aryl HydrocarbonchemistryBenzothiazoleCell Line TumorDrug Discoverybiology.proteinHumansMolecular MedicineStructure–activity relationshipBenzopyransBenzothiazolesGrowth inhibitionJournal of Medicinal Chemistry
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Synthesis and Evaluation of a Novel Series of Pyrrolizine Derivatives as Dual Cyclooxygenase-1 and 5-Lipoxygenase Inhibitors

1997

The aim of our study was to investigate structure activity relationship following the replacement of the 6-phenyl substituent at the 6,7-diaryl-2,3-dihydropyrrolizine template by various heteroaromatic residues. In this context we developed a new, efficient, and highly sensitive test method for the screening of dual cyclooxygenase-1 (COX-1) and 5-lipoxygenase (5-LOX) inhibitors. We used human platelets as a source of COX-1 and human PMNLs as a source of 5-LOX. Both cell types were isolated from the same volume of blood. PGE2 and LTB4 respectively were determined by highly selective and sensitive ELISA kits, using monoclonal antibodies. For a single determination at most 0.5 mL whole blood i…

Blood PlateletsMaleNeutrophilsmedicine.drug_classPharmaceutical ScienceContext (language use)Monoclonal antibodyChemical synthesisDrug DiscoverymedicineHumansStructure–activity relationshipCyclooxygenase InhibitorsPyrrolesLipoxygenase InhibitorsWhole bloodArachidonate 5-LipoxygenasebiologyChemistryMembrane ProteinsIn vitroIsoenzymesBiochemistryProstaglandin-Endoperoxide SynthasesEnzyme inhibitorArachidonate 5-lipoxygenaseCyclooxygenase 1biology.proteinFemaleArchiv der Pharmazie
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Non-steroidal Anti-inflammatory Agents, Part 19:E-2-Pyrrolizin-5-yl Acrylic Acids as Potent Dual or Selective Inhibitors of Bovine Cyclooxygenase and…

1995

The pyrrolizinyl substituted acrylic acid derivatives represent another class of dual and selective inhibitors of cyclooxygenase and 5-lipoxygenase. By modifying their substitution pattern at the phenyl moiety of C-6 the balance between the activity against cyclooxygenase and against 5-lipoxygenase can be shifted. Structure-activity relationships are discussed. Compound 6k is the most potent and well-balanced dual inhibitor of both enzymes, while the highest selectivity of lipoxygenase inhibition was found for 6j. The activity and selectivity of compounds with an additional sulfur moiety depend on the oxidation status of this atom, giving an indication of the discussed coupling between pero…

Blood PlateletsNeutrophilsStereochemistryCarboxylic acidPharmaceutical ScienceIn Vitro TechniquesSulfoneStructure-Activity Relationshipchemistry.chemical_compoundLipoxygenaseDrug DiscoveryAnimalsStructure–activity relationshipMoietyCyclooxygenase InhibitorsPyrrolesLipoxygenase Inhibitorschemistry.chemical_classificationbiologyAnti-Inflammatory Agents Non-SteroidalAcrylateschemistryEnzyme inhibitorArachidonate 5-lipoxygenasebiology.proteinCattleCyclooxygenaseArchiv der Pharmazie
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Cyclooxygenase-1/2 (COX-1/COX-2) and 5-lipoxygenase (5-LOX) inhibitors of the 6,7-diaryl-2,3-1H-dihydropyrrolizine type

2003

A series of 6,7-diaryl-2,3-1H-dihydropyrrolizines was prepared as COX-1/COX-2 and 5-LOX inhibitors. The inhibition of COX-1 was evaluated using intact bovine platelets as the enzyme source, whereas LPS-stimulated human monocytes served as the enzyme source for inducible COX-2. The determination of arachidonic metabolites was performed by HPLC for COX-1 and RIA for COX-2. The balance between COX-1/COX-2 and 5-LOX inhibition can be shifted by modifying the substitution pattern of the phenyl moiety at the 6- and 7-position of the pyrrolizine nucleus. Structure-activity relationships are discussed.

Blood PlateletsRadioimmunoassayHigh-performance liquid chromatographyIsozymeMonocytesDrug DiscoverymedicineCox 1 cox 2AnimalsHumansMoietyStructure–activity relationshipPyrrolesPlateletLipoxygenase InhibitorsEnzyme InhibitorsChromatography High Pressure LiquidPharmacologychemistry.chemical_classificationbiologyChemistryOrganic ChemistryMembrane ProteinsGeneral MedicineIn vitroIsoenzymesmedicine.anatomical_structureEnzymeBiochemistryCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesEnzyme inhibitorDrug DesignArachidonate 5-lipoxygenaseCyclooxygenase 1biology.proteinCattleCyclooxygenaseNucleusEuropean Journal of Medicinal Chemistry
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Inhibitory effects oftrans-resveratrol analogs molecules on the proliferation and the cell cycle progression of human colon tumoral cells

2008

International audience; Resveratrol may function as a cancer chemopreventive agent. However, few data are available on the antitumoral activities of its dimer, epsilon-viniferin, also present in human diet. So, the effects of resveratrol, epsilon-viniferin, of their acetylated forms (resveratrol triacetate, epsilon-viniferin pentaacetate) and of vineatrol (a wine grape extract) were compared on human adenocarcinoma colon cells. Resveratrol and resveratrol triacetate inhibit cell proliferation and arrest cell cycle. epsilon-Viniferin and epsilon-viniferin pentaacetate slightly reduce cell proliferation. Vineatrol inhibits cell proliferation and favors an accumulation in the S phase of the ce…

Cell Membrane Permeabilityendocrine system diseasesvineatrolMESH: Cell CycleMESH: DNA ReplicationMESH: Flow CytometryresveratrolResveratrolMESH : Antineoplastic Agents PhytogenicWine grapechemistry.chemical_compoundMESH: Structure-Activity RelationshipMESH: StilbenesStilbenesMESH : Structure-Activity RelationshipMESH: Cell Membrane Permeabilityskin and connective tissue diseasesfood and beveragesDNA NeoplasmMESH : Cell DivisionCell cycleFlow CytometryMESH : Colonic Neoplasmscolon cancerBiochemistryColonic NeoplasmsMESH: Cell Divisioncell cycleMESH : DNA NeoplasmCell Divisionhormones hormone substitutes and hormone antagonistsMESH : DNA ReplicationBiotechnologyDNA ReplicationMESH: XenobioticsMESH: Cell Line TumorMESH : Flow CytometryMESH: Antineoplastic Agents PhytogenicMESH: DNA NeoplasmMESH : XenobioticsBiologyXenobioticsMESH : StilbenesStructure-Activity RelationshipCell Line TumorMESH : Cell Cycle[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyHumansStructure–activity relationship[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologypolyphenolsS phaseMESH: Colonic NeoplasmsMESH: HumansMESH : Cell Line TumorCell growthorganic chemicalsMESH : HumansAntineoplastic Agents PhytogenicchemistryMESH : Cell Membrane PermeabilityAcetylationCell cultureCancer researchFood ScienceMolecular Nutrition & Food Research
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Ensemble-based ADME-Tox profiling and virtual screening for the discovery of new inhibitors of the Leishmania mexicana cysteine protease CPB2.8ΔCTE

2018

Abstract: In an effort to identify novel molecular warheads able to inhibit Leishmania mexicana cysteine protease CPB2.8CTE, fused benzo[b]thiophenes and ,'-triketones emerged as covalent inhibitors binding the active site cysteine residue. Enzymatic screening showed a moderate-to-excellent activity (12%-90% inhibition of the target enzyme at 20m). The most promising compounds were selected for further profiling including in vitro cell-based assays and docking studies. Computational data suggest that benzo[b]thiophenes act immediately as non-covalent inhibitors and then as irreversible covalent inhibitors, whereas a reversible covalent mechanism emerged for the 1,3,3'-triketones with a Y-to…

Cell SurvivalLeishmania mexicanaProtozoan ProteinsADME-Tox; Benzo[b]thiophenes; Cysteine protease; Leishmaniasis; TriketonesThiophenesCysteine Proteinase Inhibitors010402 general chemistry01 natural sciencesBiochemistryLeishmania mexicanaCysteine Proteinase InhibitorsCell LineInhibitory Concentration 50Structure-Activity RelationshipCysteine ProteasesCatalytic DomainDrug DiscoveryHumansStructure–activity relationshipcysteine proteaseBinding siteADME-Tox; benzo[b]thiophenes; cysteine protease; leishmaniasis; triketones; Biochemistry; Molecular MedicineBiologyleishmaniasisPharmacologychemistry.chemical_classificationVirtual screeningBinding Sitesbiology010405 organic chemistryPharmacology. TherapyOrganic Chemistrytriketonesbiology.organism_classificationCysteine protease0104 chemical sciencesMolecular Docking SimulationChemistryEnzymeBiochemistrychemistryDocking (molecular)ADME-ToxMolecular Medicinebenzo[b]thiophenes
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Comparative analysis of virtual screening approaches in the search for novel EphA2 receptor antagonists

2015

The EphA2 receptor and its ephrin-A1 ligand form a key cell communication system, which has been found overexpressed in many cancer types and involved in tumor growth. Recent medicinal chemistry efforts have identified bile acid derivatives as low micromolar binders of the EphA2 receptor. However, these compounds suffer from poor physicochemical properties, hampering their use in vivo. The identification of compounds able to disrupt the EphA2-ephrin-A1 complex lacking the bile acid scaffold may lead to new pharmacological tools suitable for in vivo studies. To identify the most promising virtual screening (VS) protocol aimed at finding novel EphA2 antagonists, we investigated the ability of…

Cell signalingDatabases Pharmaceuticaldrug designPharmaceutical ScienceComputational biologyBiologyCrystallography X-RayMolecular Docking SimulationArticleAnalytical Chemistrylcsh:QD241-441Structure-Activity RelationshipUser-Computer Interfacelcsh:Organic chemistryPPI inhibitorsDrug Discoveryshape screeningStructure–activity relationshipPhysical and Theoretical ChemistryReceptorProtein Kinase InhibitorsVirtual screeningMolecular StructureDrug discoveryReceptor EphA2EphA2 antagonistOrganic ChemistryEphrin-A1virtual screeningEPH receptor A2C700Combinatorial chemistryMolecular Docking SimulationUniPR129Chemistry (miscellaneous)Docking (molecular)dockingMolecular Medicinepharmacophore search
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Pyrrolo[2',3':3,4]cyclohepta[1,2-d][1,2]oxazoles, a New Class of Antimitotic Agents Active against Multiple Malignant Cell Types

2020

A new class of pyrrolo[2',3':3,4]cyclohepta[1,2-d][1,2]oxazoles was synthesized for the treatment of hyperproliferative pathologies, including neoplasms. The new compounds were screened in the 60 human cancer cell lines of the NCI drug screen and showed potent activity with GI50 values reaching the nanomolar level, with mean graph midpoints of 0.08-0.41 μM. All compounds were further tested on six lymphoma cell lines, and eight showed potent growth inhibitory effects with IC50 values lower than 500 nM. Mechanism of action studies showed the ability of the new [1,2]oxazoles to arrest cells in the G2/M phase in a concentration dependent manner and to induce apoptosis through the mitochondrial…

CellsMitosisAntineoplastic AgentsApoptosisAntimitotic AgentsDrug Screening Assays[12]oxazoles antimitotic agents lymphoma tubulin polymerization inhibitorsDose-Response RelationshipStructure-Activity Relationshipchemistry.chemical_compoundModelsDrug DiscoverymedicineHumansStructure–activity relationshipColchicineOxazolesAntimitotic Agents; Antineoplastic Agents; Apoptosis; Cell Proliferation; Cells Cultured; Dose-Response Relationship Drug; Drug Screening Assays Antitumor; G2 Phase Cell Cycle Checkpoints; HeLa Cells; Humans; Mitosis; Models Molecular; Molecular Structure; Oxazoles; Structure-Activity RelationshipCell Proliferationchemistry.chemical_classificationReactive oxygen speciesCulturedMolecular StructureChemistryMolecularDepolarizationAntitumorMolecular biologyG2 Phase Cell Cycle CheckpointsMechanism of actionApoptosisCell cultureMolecular MedicineAntimitotic AgentDrugmedicine.symptomHeLa Cells
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Application of molecular topology in the prediction of new compounds with anti-trypanosomal cytotoxic activity

2021

La enfermedad de Chagas es una antropozoonosis parasitaria de transmisión mayoritariamente vectorial. Si bien afecta principalmente a América, constituye una de las mayores enfermedades desatendidas a nivel mundial. Solamente dos fármacos con un alto grado de toxicidad se encuentran disponibles para su tratamiento, por lo que es preciso aunar esfuerzos en pos del desarrollo de nuevas drogas antitripanosomales eficaces y con escasos efectos adversos. En este estudio, se aplicó la topología molecular para el desarrollo de un modelo QSAR capaz de predecir la actividad citotóxica antitripanosomal de un grupo de 39 compuestos. El modelo desarrollado mediante análisis lineal discriminante permiti…

Chagas diseaseQuantitative structure–activity relationshipComputational biologyBiologyLinear discriminant analysismedicine.diseaseAntiparasiticsAntiparasitariosChagas3209 Farmacología23 QuímicamedicinePotencyMultiple linear regression analysisMolecular topologyNereis. Interdisciplinary Ibero-American Journal of Methods, Modelling and Simulation.
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Effect of EDTA and citrate on the functional activity of the first component of complement, C1, and the C1q subcomponent.

1985

The first component of complement, C1, is a calcium-dependent complex of the three distinct subcomponents, C1q, C1r, and C1s. Earlier observations revealed that treatment of C1 with EDTA led to a loss of hemolytic C1 activity even after recalcification. Therefore, it was of interest to study whether EDTA has an additional effect on C1 and its subcomponents, beside its chelating capacity. The chelating effect of EDTA was compared to that of citrate. It was found that treatment of C1 or C1 with EDTA followed by addition of Ca++ led to a loss of hemolytic activity up to 90%, depending on EDTA concentration. Even pretreatment of EDTA with varying amounts of Ca++ did not prevent the inactivation…

Chemical PhenomenaComplement Activating EnzymesMacromolecular SubstancesImmunologyKineticschemistry.chemical_elementCalciumHemolysisDissociation (chemistry)Structure-Activity RelationshipComplement C1medicineImmunology and AllergyStructure–activity relationshipHumansChelationCitratesComplement C1qEdetic AcidComplement C1qHematologymedicine.diseaseHemolysisChemistryKineticsBiochemistrychemistryEdetic AcidCalciumImmunobiology
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