Search results for "Structure-Activity Relationship"

showing 10 items of 743 documents

Optimization of Triazine Nitriles as Rhodesain Inhibitors: Structure-Activity Relationships, Bioisosteric Imidazopyridine Nitriles, and X-ray Crystal…

2013

The cysteine protease rhodesain of Trypanosoma brucei parasites causing African sleeping sickness has emerged as a target for the development of new drug candidates. Based on a triazine nitrile moiety as electrophilic headgroup, optimization studies on the substituents for the S1, S2, and S3 pockets of the enzyme were performed using structure-based design and resulted in inhibitors with inhibition constants in the single-digit nanomolar range. Comprehensive structure-activity relationships clarified the binding preferences of the individual pockets of the active site. The S1 pocket tolerates various substituents with a preference for flexible and basic side chains. Variation of the S2 subs…

Models MolecularImidazopyridineMolecular modelNitrilePyridinesStereochemistryCathepsin LTrypanosoma brucei bruceiSubstituentCysteine Proteinase InhibitorsCrystallography X-RayLigandsBiochemistryStructure-Activity Relationshipchemistry.chemical_compoundParasitic Sensitivity TestsNitrilesDrug DiscoveryHumansMoietyGeneral Pharmacology Toxicology and PharmaceuticsTriazinePharmacologyDose-Response Relationship DrugMolecular StructurebiologyTriazinesChemistryLigandOrganic ChemistryImidazolesActive siteCysteine Endopeptidasesbiology.proteinMolecular MedicineChemMedChem
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1,2,4-Oxadiazole Topsentin Analogs with Antiproliferative Activity against Pancreatic Cancer Cells, Targeting GSK3β Kinase.

2021

A new series of topsentin analogs, in which the central imidazole ring of the natural lead was replaced by a 1,2,4- oxadiazole moiety, was efficiently synthesized. All derivatives were pre-screened for antiproliferative activity against the National Cancer Institute (NCI-60) cell lines panel. The five most potent compounds were further investigated in various pancreatic ductal adenocarcinoma (PDAC) cell lines, including SUIT-2, Capan-1, and Panc-1 cells, eliciting EC50 values in the micromolar and sub-micromolar range, associated with significant reduction of cell migration. These remarkable results might be explained by the effects of these new topsentin analogues on epithelial-to-mesenchy…

Models MolecularIndoles124-oxadiazole topsentin analogs; GSK3β kinase; inhibition of migration; PDAC antiproliferative activity; proapoptotic activityApoptosisDrug Screening Assays01 natural sciencesBiochemistrychemistry.chemical_compound124-oxadiazole topsentin analogs; GSK3β kinase; PDAC antiproliferative activity; inhibition of migration; proapoptotic activity; Antineoplastic Agents; Apoptosis; Cell Proliferation; Cell Survival; Dose-Response Relationship Drug; Drug Screening Assays Antitumor; Glycogen Synthase Kinase 3 beta; Humans; Imidazoles; Indoles; Models Molecular; Molecular Structure; Oxadiazoles; Pancreatic Neoplasms; Protein Kinase Inhibitors; Structure-Activity Relationship; Tumor Cells CulturedModelsAnnexinDrug DiscoveryTumor Cells CulturedGSK3β kinaseGeneral Pharmacology Toxicology and Pharmaceutics4-oxadiazole topsentin analogsOxadiazolesCulturedMolecular StructureChemistryKinaseImidazolesCell migrationTumor Cellsinhibition of migrationMolecular MedicineDrugIntracellularPDAC antiproliferative activityproapoptotic activityCell Survival12Antineoplastic AgentsDose-Response RelationshipStructure-Activity RelationshipPancreatic cancermedicineHumansPropidium iodideProtein Kinase InhibitorsCell ProliferationPharmacologyGlycogen Synthase Kinase 3 betaDose-Response Relationship Drug010405 organic chemistryOrganic ChemistryMolecularAntitumormedicine.diseaseSettore CHIM/08 - Chimica FarmaceuticaMolecular biology0104 chemical sciencesPancreatic Neoplasms010404 medicinal & biomolecular chemistryApoptosisCell cultureDrug Screening Assays Antitumor124-oxadiazole topsentin analogChemMedChem
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Synthesis, Anti-Inflammatory Activity, and in Vitro Antitumor Effect of a Novel Class of Cyclooxygenase Inhibitors: 4-(Aryloyl)phenyl Methyl Sulfones

2010

Following our previous research on anti-inflammatory drugs (NSAIDs), we report on the design and synthesis of 4-(aryloyl)phenyl methyl sulfones. These substances were characterized for their capacity to inhibit cyclooxygenase (COX-1 and COX-2) isoenzymes. Molecular modeling studies showed that the methylsulfone group of these compounds was inserted deep in the pocket of the human COX-2 binding site, in an orientation that precludes hydrogen bonding with Arg120, Ser353, and Tyr355 through their oxygen atoms. The N-arylindole 33 was the most potent inhibitor of COX-2 and also the most selective (COX-1/COX-2 IC(50) ratio was 262). The indole derivative 33 was further tested in vivo for its ant…

Models MolecularIndolesMolecular modelCell SurvivalStereochemistrymedicine.drug_classAntineoplastic AgentsAnti-inflammatoryStructure-Activity RelationshipIn vivoCell Line TumorDrug DiscoverymedicineAnimalsHumansCyclooxygenase InhibitorsSulfonesBinding siteIC50Cell ProliferationIndole testCyclooxygenase 2 InhibitorsbiologyChemistryStereoisomerismSettore CHIM/08 - Chimica FarmaceuticaIn vitroRats4-(Aryloyl)phenyl methyl sulfones anti-inflammatory activity antitumor effect COX-1/COX-2 selectivityCyclooxygenase 1biology.proteinThermodynamicsMolecular MedicineCyclooxygenaseDrug Screening Assays AntitumorHydrophobic and Hydrophilic InteractionsJournal of Medicinal Chemistry
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Synthesis and Biological Evaluation of 1-Methyl-2-(3',4',5'-trimethoxybenzoyl)-3-aminoindoles as a New Class of Antimitotic Agents and Tubulin Inhibi…

2008

The 2-(3,4,5-trimethoxybenzoyl)-2-aminoindole nucleus was used as the fundamental structure for the synthesis of compounds modified with respect to positions C-4 to C-7 with different moieties (chloro, methyl, or methoxy). Additional structural variations concerned the indole nitrogen, which was alkylated with small alkyl groups such as methyl or ethyl. We have identified 1-methyl-2-(3,4,5-trimethoxybenzoyl)-3-amino-7-methoxyindole as a new highly potent antiproliferative agent that targets tubulin at the colchicine binding site and leads to apoptotic cell death.

Models MolecularIndolesStereochemistryAlkylationAntimitotic AgentsChemical synthesisMiceStructure-Activity RelationshipBiopolymersTubulinCell Line TumorDrug DiscoveryStructure–activity relationshipAnimalsHumansIndole testBinding SitesbiologyTubulin ModulatorsChemistryBiological activityTubulin ModulatorsTubulinbiology.proteinMolecular MedicineAntimitotic AgentDrug Screening Assays AntitumorColchicineProtein Binding
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Variations of acidic functions at position 2 and substituents at positions 4, 5 and 6 of the indole moiety and their effect on NMDA-glycine site affi…

2003

The synthetic procedures to obtain indole derivatives with different acidic functions at position 2 of the indole are reported. The synthesised and tested derivatives comprise 5-tetrazolyl, 1,3,4-oxadiazol-5-yl-2-one, and indole-2-carboxylic acid amides with 5-aminotetrazole, methanesulphonamide and trifluoromethanesulphonamide moieties. The binding affinity was evaluated using [3H]MDL 105,519 and pig cortical brain membranes. In general, compounds with acidic functions different from a carboxylic acid moiety are less potent than indole-2-carboxylic acid derivatives. Also, the 4,6-dichloro substitution pattern was compared to 5-tert-butyl derivatives and compounds not substituted in the ben…

Models MolecularIndolesSwineStereochemistryCarboxylic acidGlycineReceptors N-Methyl-D-AspartateChemical synthesisInhibitory Concentration 50Radioligand AssayStructure-Activity Relationshipchemistry.chemical_compoundDrug DiscoveryAnimalsMoietyBenzeneImideCerebral CortexPharmacologyIndole testchemistry.chemical_classificationBinding SitesBicyclic moleculeCell MembraneOrganic ChemistryGeneral MedicineLigand (biochemistry)MembranechemistryGlycineHydantoin derivativesNMDA receptorEuropean Journal of Medicinal Chemistry
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Design, Synthesis, and Biological Evaluation of 3,4-Diarylmaleimides as Angiogenesis Inhibitors

2006

The new analogue 2 of combretastatin A-4 was discovered to be an inhibitor of tubulin polymerization with an IC50 of 7.6 microM and reduced angiogenesis in the in vivo chick embryo model. Interestingly, in a series of 2,3-diarylmaleimides closely related to this lead, no other compound was found to be active in the tubulin polymerization assay. However, by screening in the in vivo chick embryo assay 10 was identified as a potent angiogenesis inhibitor indicating an alternative target. Indeed, molecular modeling studies suggest a reasonable binding mode of 10 at the ATP-binding site of the model kinase CDK2. Motivated by these results, analogues of 10 were screened for inhibitory activity in…

Models MolecularIndolesanimal structuresAngiogenesisAngiogenesis InhibitorsChick EmbryoIn Vitro TechniquesMaleimidesStructure-Activity Relationshipchemistry.chemical_compoundAdenosine TriphosphateIn vivoDrug DiscoveryAnimalsStructure–activity relationshipPyrrolesBinding siteCombretastatinBinding SitesbiologyChemistryKinaseCyclin-dependent kinase 2Vascular Endothelial Growth Factor Receptor-2Angiogenesis inhibitorBiochemistryDrug Designbiology.proteinMolecular MedicineJournal of Medicinal Chemistry
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Snake venom disintegrins: evolution of structure and function.

2005

Disintegrins represent a family of polypeptides present in the venoms of various vipers that selectively block the function of integrin receptors. Here, we review our current view and hypothesis on the emergence and the structural and functional diversification of disintegrins by accelerated evolution and the selective loss of disulfide bonds of duplicated genes. Research on disintegrins is relevant for understanding the biology of viper venom toxins, but also provides information on new structural determinants involved in integrin recognition that may be useful in basic and clinical research. The role of the composition, conformation, and dynamics of the integrin inhibitory loop acting in …

Models MolecularIntegrinsStereochemistryDisintegrinsIntegrinAmino Acid MotifsMolecular Sequence DataSequence alignmentVenomToxicologyViper VenomsEvolution MolecularStructure-Activity RelationshipProtein structureGenes DuplicateAnimalsAmino Acid SequencePeptide sequencePhylogenybiologyBase SequenceSnakesCell biologyProtein Structure TertiarySnake venombiology.proteinSequence AlignmentFunction (biology)Snake VenomsToxicon : official journal of the International Society on Toxinology
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Antimicrobial Peptides and Their Superior Fluorinated Analogues: Structure-Activity Relationships as Revealed by NMR Spectroscopy and MD Calculations

2010

9 pag., 6 fig, 3 tab.

Models MolecularMagnetic Resonance SpectroscopyHalogenationProtein ConformationDiffusionAntimicrobial peptidesMicrobial Sensitivity TestsMolecular Dynamics SimulationBiochemistryMicelleStructure-Activity RelationshipMolecular dynamicsantimicrobial peptidesNMR spectroscopyComputational chemistryfluorineEscherichia coliOrganic chemistryAmino Acid SequenceMolecular BiologyAqueous solutionMolecular StructureChemistryOrganic ChemistrySodium Dodecyl SulfateWaterNuclear magnetic resonance spectroscopyAntimicrobialmolecular dynamicsSolutionsMembranemembranespeptidesMolecular MedicineAntimicrobialSDS micellesOligopeptidesAntimicrobial Cationic Peptides
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The Nature of the Stimulus and of the Fumarate Binding Site of the Fumarate Sensor DcuS of Escherichia coli

2005

DcuS is a membrane-associated sensory histidine kinase of Escherichia coli specific for C(4) -dicarboxylates. The nature of the stimulus and its structural prerequisites were determined by measuring the induction of DcuS-dependent dcuB'-'lacZ gene expression. C(4)-dicarboxylates without or with substitutions at C2/C3 by hydrophilic (hydroxy, amino, or thiolate) groups stimulated gene expression in a similar way. When one carboxylate was replaced by sulfonate, methoxy, or nitro groups, only the latter (3-nitropropionate) was active. Thus, the ligand of DcuS has to carry two carboxylate or carboxylate/nitro groups 3.1-3.8 A apart from each other. The effector concentrations for half-maximal i…

Models MolecularMagnetic Resonance SpectroscopyHistidine KinaseRecombinant Fusion ProteinsMolecular Sequence Datamedicine.disease_causeBiochemistryCitric AcidStructure-Activity Relationshipchemistry.chemical_compoundFumaratesEscherichia colimedicineDicarboxylic AcidsAmino Acid SequenceCarboxylatePhosphorylationBinding siteKinase activityTartratesMolecular BiologyEscherichia coliPeptide sequenceDicarboxylic Acid TransportersBinding SitesChemistryEscherichia coli ProteinsAutophosphorylationHistidine kinaseGene Expression Regulation BacterialCell BiologyNitro CompoundsPeptide FragmentsEnzyme ActivationLac OperonBiochemistryMutagenesis Site-DirectedPropionatesProtein KinasesSequence AlignmentBinding domainJournal of Biological Chemistry
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3-Aryl-2-[1H-benzotriazol-1-yl]acrylonitriles: a novel class of potent tubulin inhibitors.

2011

During a screening for compounds that could act against Mycobacterium tuberculosis, a series of new cellular antiproliferative agents was identified. The most cytotoxic molecules were evaluated against a panel of human cell lines derived from hematological and solid human tumors. In particular, (E)-2-(1H-benzo[d] [1,2,3]triazol-1-yl)-3-(4-methoxyphenyl)acrylonitrile (1) was found to be of a potency comparable to etoposide and greater than 6-mercaptopurine in all cell lines tested. Accordingly, a synthesis of a new series of (E)-2-(5,6-dichloro-1H-benzo[d] [1,2,3]triazol-1-yl)-3-(4-R-phenyl)acrylonitriles was conducted in order to extend the studies of structure-activity relationship (SAR) f…

Models MolecularMagnetic Resonance SpectroscopyMolecular modelStereochemistryAnti-cancer drugsBinding CompetitiveGas Chromatography-Mass SpectrometryAnti-cancer drugchemistry.chemical_compoundStructure-Activity RelationshipTubulinAnti-cancer drugs; drug design and development; computer assisted drug designDrug DiscoveryK562 CellmedicineStructure–activity relationshipHumansdrug design and developmentPharmacologybiologyAcrylonitrileChemistryArylOrganic ChemistryCell Cyclecomputer assisted drug designGeneral MedicineCell cycleTriazolesTubulinPodophyllotoxinCell cultureTubulin Binding Agentbiology.proteinTriazoleColchicineK562 CellsHumanmedicine.drugEuropean journal of medicinal chemistry
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