Search results for "Enzyme Assays"

showing 10 items of 22 documents

Discovery of benzimidazole-based Leishmania mexicana cysteine protease CPB2.8ΔCTE inhibitors as potential therapeutics for leishmaniasis

2018

Abstract: Chemotherapy is currently the only effective approach to treat all forms of leishmaniasis. However, its effectiveness is severely limited due to high toxicity, long treatment length, drug resistance, or inadequate mode of administration. As a consequence, there is a need to identify new molecular scaffolds and targets as potential therapeutics for the treatment of this disease. We report a small series of 1,2‐substituted‐1H‐benzo[d]imidazole derivatives (9ad) showing affinity in the submicromolar range (Ki = 0.150.69 μM) toward Leishmania mexicanaCPB2.8ΔCTE, one of the more promising targets for antileishmanial drug design. The compounds confirmed activity in vitro against intrace…

BenzimidazoleCell SurvivalIn silicoLeishmania mexicanaAntiprotozoal AgentsDrug Evaluation PreclinicalProtozoan ProteinsDrug resistanceCysteine Proteinase InhibitorsPharmacologyAntileishmanial agents Benzimidazole derivatives Docking studies In silico profiling Leishmania mexicanaCPB2.8 Biochemistry Molecular Medicine01 natural sciencesBiochemistryLeishmania mexicanaCell LineInhibitory Concentration 50chemistry.chemical_compoundCysteine ProteasesDrug DiscoverymedicineHumansAmastigoteLeishmaniasisBiologyEnzyme AssaysPharmacologyBinding Sitesbiology010405 organic chemistryChemistryPharmacology. TherapyOrganic ChemistryHydrogen BondingLeishmaniasisbiology.organism_classificationmedicine.diseaseLeishmaniaProtein Structure Tertiary0104 chemical sciencesMolecular Docking Simulation010404 medicinal & biomolecular chemistryChemistryMolecular MedicineBenzimidazolesHuman medicineLeishmania infantumChemical biology and drug design
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Amperometric detection of extended-spectrum β-lactamase activity : application to the characterization of resistant E.coli strains

2015

EA MERS CT3; International audience; The amperometric detection of extended-spectrum β-lactamase (ESBL) with carbon screen-printed sensors was investigated in the presence of the Nitrocefin, a commercially-available β-lactamase chromogenic cephalosporin substrate. Using an ESBL isolated from a clinical sample, it was shown for the first time that the intensity of a specific anodic pic current (EP = [similar]+0.3 V vs. Ag/AgCl) resulting from the catalytic hydrolysis of the β-lactam ring was proportional to the amount of ESBL. The proof-of-principle of a novel susceptibility assay for the rapid and accurate identification of ESBL- producing bacteria was then demonstrated. The detection schem…

Cefotaximemedicine.drug_classélectrochimie[SDV]Life Sciences [q-bio]CephalosporinAnalytical chemistryBiochemistrybeta-LactamasesAnalytical Chemistry03 medical and health sciencesClavulanic acidDrug Resistance BacterialElectrochemistrymedicineEscherichia colipolycyclic compoundsEnvironmental ChemistryNitrocefin[SDV.BV]Life Sciences [q-bio]/Vegetal Biologyélectrode sérigraphiéeSpectroscopybêta-lactamase à spectre étendu (BLSE)Enzyme Assays030304 developmental biologyDetection limit0303 health sciencesChromatographybiology030306 microbiologyChemistryChromogenicbactériologienitrocéfineHydrolysisbiochemical phenomena metabolism and nutritionbiology.organism_classificationbacterial infections and mycosesAmperometryAnti-Bacterial AgentsCephalosporinscultureampérométrie[SDE]Environmental SciencesBacteriamedicine.drugbactériologie;culture;Escherichia coli;bêta-lactamase à spectre étendu (BLSE);électrochimie;ampérométrie;électrode sérigraphiée;nitrocéfine
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Binding and/or hydrolysis of purine‐based nucleotides is not required for IM30 ring formation

2021

IM30, the inner membrane-associated protein of 30 kDa, is conserved in cyanobacteria and chloroplasts. Although its exact physiological function is still mysterious, IM30 is clearly essential for thylakoid membrane biogenesis and/or dynamics. Recently, a cryptic IM30 GTPase activity has been reported, albeit thus far no physiological function has been attributed to this. Yet, it is still possible that GTP binding/hydrolysis affects formation of the prototypical large homo-oligomeric IM30 ring and rod structures. Here, we show that the Synechocystis sp. PCC 6803 IM30 protein in fact is an NTPase that hydrolyzes GTP and ATP, but not CTP or UTP, with about identical rates. While IM30 forms lar…

GTP'Genetic VectorsBiophysicsGene ExpressionGTPaseRing (chemistry)ThylakoidsBiochemistrySubstrate Specificity03 medical and health sciencesAdenosine TriphosphateBacterial ProteinsStructural BiologyEscherichia coliGeneticsNucleotideddc:610Cloning MolecularMolecular BiologyEnzyme Assays030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryHydrolysis030302 biochemistry & molecular biologySynechocystisSynechocystisMembrane ProteinsCell BiologyNucleoside-Triphosphatasebiology.organism_classificationRecombinant ProteinsKineticsMicroscopy ElectronThylakoidMembrane biogenesisBiophysicsGuanosine TriphosphateBiogenesisProtein BindingFEBS Letters
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Fluorovinylsulfones and -Sulfonates as Potent Covalent Reversible Inhibitors of the Trypanosomal Cysteine Protease Rhodesain: Structure–Activity Rela…

2021

Rhodesain is a major cysteine protease of Trypanosoma brucei rhodesiense, a pathogen causing Human African Trypanosomiasis, and a validated drug target. Recently, we reported the development of α-halovinylsulfones as a new class of covalent reversible cysteine protease inhibitors. Here, α-fluorovinylsulfones/-sulfonates were optimized for rhodesain based on molecular modeling approaches. 2d, the most potent and selective inhibitor in the series, shows a single-digit nanomolar affinity and high selectivity toward mammalian cathepsins B and L. Enzymatic dilution assays and MS experiments indicate that 2d is a slow-tight binder (Ki = 3 nM). Furthermore, the nonfluorinated 2d-(H) shows favorabl…

MaleBiodistributionVinyl CompoundsMolecular modelTrypanosoma brucei bruceiCysteine Proteinase InhibitorsMiceStructure-Activity RelationshipParasitic Sensitivity TestsIn vivoDrug DiscoveryAnimalsHumansStructure–activity relationshipSulfonesEnzyme Assayschemistry.chemical_classificationMolecular StructureChemistryTrypanosoma brucei rhodesienseTrypanocidal AgentsCysteine proteaseMolecular Docking SimulationCysteine EndopeptidasesKineticsEnzymeBiochemistryCovalent bondMolecular MedicineFemaleSulfonic AcidsHeLa CellsProtein BindingJournal of Medicinal Chemistry
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Estradiol induces endothelial cell migration and proliferation through estrogen receptor-enhanced RhoA/ROCK pathway

2010

Migration and proliferation of endothelial cells are involved in re-endothelialization and angiogenesis, two important cardiovascular processes that are increased in response to estrogens. RhoA, a small GTPase which controls multiple cellular processes, is involved in the control of cell migration and proliferation. Our aim was to study the role of RhoA on estradiol-induced migration and proliferation and its dependence on estrogen receptors activity. Human umbilical vein endothelial cells were stimulated with estradiol, in the presence or absence of ICI 182780 (estrogen receptors antagonist) and Y-27632 (Rho kinase inhibitor). Estradiol increased Rho GEF-1 gene expression and RhoA (gene an…

MaleTranscriptional ActivationRHOAAngiogenesismedicine.drug_classEstrogen receptorCell Cycle ProteinsBiochemistryUmbilical CordEndocrinologyCell MovementmedicineHumansReceptorMolecular BiologyCells CulturedCell ProliferationEnzyme Assaysrho-Associated KinasesEstradiolbiologyChemistryEndothelial CellsCell migrationUp-RegulationCell biologyEndothelial stem cellReceptors EstrogenRho kinase inhibitorEstrogenCancer researchbiology.proteinFemalerhoA GTP-Binding Proteinhormones hormone substitutes and hormone antagonistsSignal TransductionMolecular and Cellular Endocrinology
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Phosphonic Acid Analogs of Fluorophenylalanines as Inhibitors of Human and Porcine Aminopeptidases N: Validation of the Importance of the Substitutio…

2020

International audience; A library of phosphonic acid analogs of phenylalanine substituted with fluorine, chlorine and trifluoromethyl moieties on the aromatic ring was synthesized and evaluated for inhibitory activity against human (hAPN) and porcine (pAPN) aminopeptidases. Fluorogenic screening indicated that these analogs are micromolar or submicromolar inhibitors, both enzymes being more active against hAPN. In order to better understand the mode of the action of the most active compounds, molecular modeling was used. It confirmed that aminophosphonic portion of the enzyme is bound nearly identically in the case of all the studied compounds, whereas the difference in activity results fro…

Models MolecularMolecular modelPhosphorous AcidsSwineStereochemistrylcsh:QR1-502chemistry.chemical_elementPhenylalanine[CHIM.THER]Chemical Sciences/Medicinal ChemistryCD13 AntigensRing (chemistry)Biochemistrylcsh:MicrobiologyArticle03 medical and health scienceschemistry.chemical_compound0302 clinical medicinefluorineinhibitorsChlorineSide chainAnimalsHumansMolecular BiologyEnzyme Assays030304 developmental biologyphosphonic acid analogschemistry.chemical_classification0303 health sciencesTrifluoromethyl[CHIM.ORGA]Chemical Sciences/Organic chemistrymolecular modelingReproducibility of ResultsStereoisomerismMolecular Docking SimulationEnzymechemistry030220 oncology & carcinogenesishuman and porcine aminopeptidaseEnantiomerMolecules
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Proteomic identification of protease cleavage sites characterizes prime and non-prime specificity of cysteine cathepsins B, L, and S.

2011

Cysteine cathepsins mediate proteome homeostasis and have pivotal functions in diseases such as cancer. To better understand substrate recognition by cathepsins B, L, and S, we applied proteomic identification of protease cleavage sites (PICS) for simultaneous profiling of prime and non-prime specificity. PICS profiling of cathepsin B endopeptidase specificity highlights strong selectivity for glycine in P3' due to an occluding loop blocking access to the primed subsites. In P1', cathepsin B has a partial preference for phenylalanine, which is not found for cathepsins L and S. Occurrence of P1' phenylalanine often coincides with aromatic residues in P2. For cathepsin L, PICS identifies 845 …

Models MolecularProteomicsTime Factorsmedicine.medical_treatmentProteolysisCathepsin LPhenylalanineGlycineBiologyBiochemistryCathepsin BPichiaCathepsin BSubstrate SpecificityCathepsin LCathepsin OPeptide LibraryCatalytic DomainmedicineHumansCathepsin SEnzyme AssaysCathepsinProteasemedicine.diagnostic_testGeneral ChemistryHydrogen-Ion ConcentrationMolecular biologyCathepsinsHEK293 CellsBiochemistryProteolysisbiology.proteinCysteinePeptide HydrolasesProtein BindingJournal of proteome research
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Detection of a plant enzyme exhibiting chlorogenate-dependant caffeoyltransferase activity in methanolic extracts of arbuscular mycorrhizal tomato ro…

2012

When Glomus intraradices-colonised tomato roots were extracted in methanol at 6 degrees C, chlorogenic acid (5-caffeoylquinic acid), naturally present in the extract, was slowly converted by transesterification into methyl caffeate. The progress of the reaction could be monitored by HPLC. The reaction only occurred when the ground roots were left in contact with the hydro-alcoholic extract and required the presence of 15-35% water in the mixture. When the roots were extracted in ethanol, chlorogenic acid was transformed to ethyl caffeate in the same conditions. The reaction was also detected in Glomus mosseae-colonised tomato root extracts. It was also detectable in non-mycorrhizal root ext…

Physiology[SDV]Life Sciences [q-bio]Arbuscular mycorrhizal fungiPlant SciencePlant RootsSubstrate SpecificityACBIOSYNTHESISchemistry.chemical_compoundTRANSFERASESolanum lycopersicumMycorrhizaeMethyl caffeateSWEET-POTATO ROOTSFood scienceEnzyme InhibitorsGlomusChromatography High Pressure LiquidPlant ProteinsbiologyTemperaturePlant physiologyfood and beveragesChlorogenic acidBiochemistryFUNGUSCOFFEE[SDE]Environmental SciencesGENESMETABOLISMCaffeoyltransferaseTomatoCaffeic AcidsChlorogenic acidTransferasesGenetics[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyEnzyme AssaysEthanolEsterificationPlant ExtractsfungiEthyl caffeatePlant Components Aerialbiology.organism_classificationRootsEnzyme assayEnzyme ActivationPhenylmethylsulfonyl FluorideTransesterificationchemistrybiology.proteinMethanolCAFFEIC ACIDCATALYZED SYNTHESIS
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Esterase inhibition by synergists in the western flower thrips Frankliniella occidentalis.

2010

BACKGROUND: Western flower thrips (WFT), Frankliniella occidentalis (Pergande), is among the most important crop pests in the south-eastern region of Spain. Its increasing resistance to insecticides constitutes a serious problem, and understanding the mechanisms involved is therefore of great interest. Use of synergists to inhibit the enzymes involved in insecticide detoxification is widely used to determine their responsibility for insecticide resistance. However, they do not always act as intended or expected, and caution must be exercised when interpreting synergist results. RESULTS: Laboratory-selected strains of WFT were used to analyse the effects of the synergists piperonyl butoxide …

Piperonyl butoxideInsecticidesTime FactorsMethiocarbIsozymeEsteraseToxicologyInsecticide Resistancechemistry.chemical_compoundPyrethrinsAnimalsEnzyme InhibitorsIncubationEnzyme Assayschemistry.chemical_classificationbiologyOrganothiophosphatesThysanopteraEsterasesPesticide SynergistsGeneral Medicinebiology.organism_classificationEnzyme assayWestern flower thripsEnzyme ActivationIsoenzymesEnzymechemistryMethiocarbInsect Sciencebiology.proteinCarbamatesAgronomy and Crop SciencePest management science
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Study of enzymatic activity in human neuroblastoma cells SH-SY5Y exposed to zearalenone's derivates and beauvericin.

2021

Abstract Beauvericin (BEA), α-zearalenol (α-ZEL) and β-zearalenol (β-ZEL), are produced by several Fusarium species that contaminate cereal grains. These mycotoxins can cause cytotoxicity and neurotoxicity in various cell lines and they are also capable of produce oxidative stress at molecular level. However, mammalian cells are equipped with a protective endogenous antioxidant system formed by no-enzymatic antioxidant and enzymatic protective systems such as glutathione peroxidase (GPx), glutathione S-transferase (GST), catalase (CAT) and superoxide dismutase (SOD). The aim of this study was evaluating the effects of α-ZEL, β-ZEL and BEA, on enzymatic GPx, GST, CAT and SOD activity in huma…

SH-SY5YAntioxidantmedicine.medical_treatmentToxicologymedicine.disease_causeSuperoxide dismutase03 medical and health scienceschemistry.chemical_compound0404 agricultural biotechnologyCell Line TumorDepsipeptidesmedicineHumans030304 developmental biologyEnzyme AssaysGlutathione Transferasechemistry.chemical_classification0303 health sciencesGlutathione PeroxidasebiologySuperoxide DismutaseGlutathione peroxidase04 agricultural and veterinary sciencesGeneral MedicineGlutathioneMycotoxinsCatalase040401 food scienceMolecular biologyBeauvericinchemistryPeroxidasesCatalasebiology.proteinZeranolOxidative stressFood ScienceFood and chemical toxicology : an international journal published for the British Industrial Biological Research Association
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