Search results for "Protease"

showing 10 items of 463 documents

In situ formation of pyronin dyes for fluorescence protease sensing

2017

International audience; We report a reaction-based strategy for the fluorogenic detection of protease activity. Based on the "covalent-assembly" probe design principle recently put forward by the Yang group for detection of Sarin related threats (J. Am. Chem. Soc., 2014, 136, 6594-6597), we have designed two unusual nonfluorescent caged precursors (mixed bis-aryl ethers) which are readily converted into a fluorescent unsymmetrical pyronin dye through a domino cyclisation-aromatisation reaction triggered by penicillin G acylase (PGA) or leucine aminopeptidase (LAP). Fluorescence-based in vitro assays and HPLCfluorescence/- MS analyses support the claimed activation mechanism whose the furthe…

In situStereochemistrymedicine.medical_treatment010402 general chemistryalkaline-phosphatase activity01 natural sciencesBiochemistryAminopeptidaseFluorescenceMass SpectrometryIn vivo[ CHIM.ORGA ] Chemical Sciences/Organic chemistryhydrogen-sulfidemedicinePyronineturn-on chemodosimeterPhysical and Theoretical ChemistryChromatography High Pressure Liquidlarge stokes shiftFluorescent DyesProteaseMolecular Structure[CHIM.ORGA]Chemical Sciences/Organic chemistry010405 organic chemistryChemistryOrganic ChemistryFluorescence0104 chemical sciences3. Good healthselective detectionPenicillin G Acylasefluorogenic probesplacental leucine aminopeptidasesensitive detectioncascade reactionLeucineliving cellsPeptide Hydrolases
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Advocacy of targeting protease‐activated receptors in severe coronavirus disease 2019

2021

Identifying drug targets mitigating vascular dysfunction, thrombo-inflammation and thromboembolic complications in COVID-19 is essential. COVID-19 coagulopathy differs from sepsis coagulopathy. Factors that drive severe lung pathology and coagulation abnormalities in COVID-19 are not understood. Protein-protein interaction studies indicate that the tagged viral bait protein ORF9c directly interacts with PAR2, which modulates host cell IFN and inflammatory cytokines. In addition to direct interaction of SARS-CoV-2 viral protein with PARs, we speculate that activation of PAR by proteases plays a role in COVID-19-induced hyperinflammation. In COVID-19-associated coagulopathy elevated levels of…

InflammationPharmacologyChemokineProteasesbiologySARS-CoV-2business.industryReceptors Proteinase-ActivatedInflammationVascular permeabilitymedicine.diseaseArticleCOVID-19 Drug TreatmentProinflammatory cytokineSepsisCytokine release syndromeImmunologyCoagulopathybiology.proteinHumansMedicinemedicine.symptomCytokine Release SyndromebusinessBritish Journal of Pharmacology
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Development of novel dipeptide-like rhodesain inhibitors containing the 3-bromoisoxazoline warhead in a constrained conformation.

2015

Novel dipeptide-like rhodesain inhibitors containing the 3-bromoisoxazoline warhead in a constrained conformation were developed; some of them possess K(i) values in the micromolar range. We studied the structure-activity relationship of these derivatives and we performed docking studies, which allowed us to find out the key interactions established by the inhibitors with the target enzyme. Biological results indicate that the nature of the P2 and P3 substituents and their binding to the S2/S3 pockets is strictly interdependent.

InhibitorMolecular modelCell SurvivalClinical BiochemistryTrypanosoma brucei bruceiAntiprotozoal AgentsPharmaceutical ScienceMolecular modelingCysteine Proteinase InhibitorsBiochemistryCell Linechemistry.chemical_compoundMiceStructure-Activity RelationshipCysteine ProteasesDrug DiscoveryAnimalsMolecular Biology3-Bromo isoxazolinechemistry.chemical_classificationDipeptide-likeDipeptideBinding SitesOrganic ChemistryDipeptidesIsoxazolesCombinatorial chemistryProtein Structure TertiaryMolecular Docking SimulationCysteine EndopeptidasesEnzymeRhodesainchemistryWarheadDocking (molecular)Drug DesignMolecular MedicineRhodesain Dipeptide-like 3-Bromo isoxazoline Inhibitor Molecular modelingBioorganicmedicinal chemistry
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Domain shuffling between Vip3Aa and Vip3Ca: chimera stability and insecticidal activity against European, American, African, and Asian pests

2020

The bacterium Bacillus thuringiensis produces insecticidal Vip3 proteins during the vegetative growth phase with activity against several lepidopteran pests. To date, three different Vip3 protein families have been identified based on sequence identity: Vip3A, Vip3B, and Vip3C. In this study, we report the construction of chimeras by exchanging domains between Vip3Aa and Vip3Ca, two proteins with marked specificity differences against lepidopteran pests. We found that some domain combinations made proteins insoluble or prone to degradation by trypsin as most abundant insect gut protease. The soluble and trypsin-stable chimeras, along with the parental proteins Vip3Aa and Vip3Ca, were tested…

InsecticidesAsiaInsectaHealth Toxicology and Mutagenesismedicine.medical_treatmentBacillus thuringiensislcsh:MedicineSpodopteraToxicologyArticleLethal Dose 5003 medical and health sciencesHelicoverpa armigeraBacterial ProteinsProtein DomainsBacillus thuringiensismedicineAnimalsSpodoptera littoralisPest Control Biological030304 developmental biologychemistry.chemical_classification0303 health sciencesProteasebiology030306 microbiologyProtein Stabilitylcsh:RfungiSpodoptera spp.Ostrinia furnacalisSouth Americabiology.organism_classificationFusion proteinAnticarsia gemmatalisAmino acidEuropeAnticarsia gemmatalisspodoptera spp. helicoverpa armigeraBiochemistrychemistryAfricaNorth AmericaMamestra brassicaeOstrinia furnacalis
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Susceptibility of Spodoptera frugiperda and S. exigua to Bacillus thuringiensis Vip3Aa insecticidal protein

2011

The Vip3Aa protein is an insecticidal protein secreted by Bacillus thuringiensis during the vegetative stage of growth. The activity of this protein has been tested after different steps/protocols of purification using Spodoptera frugiperda as a control insect. The results showed that the Vip3Aa protoxin was stable and retained full toxicity after being subjected to common biochemical steps used in protein purification. Bioassays with the protoxin in S. frugiperda and S. exigua showed pronounced differences in LC(50) values when mortality was measured at 7 vs. 10d. At 7d most live larvae were arrested in their development. LC(50) values of "functional mortality" (dead larvae plus larvae rem…

InsecticidesLongevityBacillus thuringiensisInsect pest controlInsect proteaseBacterial ProteinSpodopteraSpodopteraMedian lethal doseMicrobiologyLethal Dose 50Vegetative insecticidal proteinBacterial ProteinsSpecies SpecificityBacillus thuringiensisparasitic diseasesExiguaProtein purificationBotanyAnimalsBacillus thuringiensiBioassayPest Control BiologicalInsecticideEcology Evolution Behavior and SystematicsbiologyAnimalfungiMidgutbiology.organism_classificationBioinsecticideHost-Pathogen InteractionMode of actionLarvaHost-Pathogen InteractionsInstarBiological AssayElectrophoresis Polyacrylamide GelDisease SusceptibilityJournal of Invertebrate Pathology
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Combining Hexanoic Acid Plant Priming with Bacillus thuringiensis Insecticidal Activity against Colorado Potato Beetle

2013

Interaction between insect herbivores and host plants can be modulated by endogenous and exogenous compounds present in the source of food and might be successfully exploited in Colorado potato beetle (CPB) pest management. Feeding tests with CPB larvae reared on three solanaceous plants (potato, eggplant and tomato) resulted in variable larval growth rates and differential susceptibility to Bacillus thuringiensis Cry3Aa toxin as a function of the host plant. An inverse correlation with toxicity was observed in Cry3Aa proteolytic patterns generated by CPB midgut brush-border membrane vesicles (BBMV) from Solanaceae-fed larvae, being the toxin most extensively proteolyzed on potato, followed…

Insecticidesmedicine.disease_causeMass Spectrometrylcsh:Chemistrychemistry.chemical_compoundHemolysin ProteinsPlant Growth RegulatorsCysteine ProteasesBacillus thuringiensisPlant defense against herbivoryColorado potato beetleElectrophoresis Gel Two-Dimensionallcsh:QH301-705.5SpectroscopySolanaceaeHexanoic acidbiologyfood and beveragesGeneral MedicineComputer Science ApplicationsColeopterasurgical procedures operativeBiochemistryLarvaHost-Pathogen Interactionsplant hormonesInsect ProteinsSolanaceaeproteolysisColoradoMolecular Sequence DataBacillus thuringiensisCatalysisArticleMicrobiologyCry3Aa toxinInorganic Chemistryintestain proteasesBacterial Proteinsplant defensemedicineAnimalsAmino Acid SequencePhysical and Theoretical ChemistryprimingMolecular BiologyCaproatesSolanum tuberosumBacillus thuringiensis ToxinsToxinOrganic ChemistryColorado potato beetlefungiBody WeightMidgutColorado potato beetle;<i> Bacillus thuringiensis</i>; Cry3Aa toxin; intestain proteases; proteolysis; Solanaceae; hexanoic acid; priming; plant defense; plant hormonesFeeding Behaviorbiology.organism_classificationDietEndotoxinsPapainchemistrylcsh:Biology (General)lcsh:QD1-999hexanoic acidPeptidesDigestive SystemSequence AlignmentInternational Journal of Molecular Sciences
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Immunological Probes for the Bradykinin B2 Receptor. A Toolbox

1997

Publisher Summary This chapter provides an overview of the immunological tools for bradykinin (BK) B 2 receptor. Receptors for kinins are classified as two major subtypes, B 1 and B 2 , although other subtypes may exist. B 1 receptors are activated by carboxyterminally truncated kinins, whereas BK and kallidin (Lys-BK) are B 2 receptor agonists. Molecular cloning has revealed the primary structures of B 1 and B 2 receptors and identified them as members of the G protein-coupled receptor family, characterized by seven membrane-spanning α-helices. In some tissues, B 1 receptor expression is induced by cytokines, such as interleukin-1, whereas the B 2 receptor is thought to be expressed consti…

Interleukin-21 receptorReceptor expressionB-cell receptor5-HT5A receptorImmune receptorGABBR1BiologyBradykinin receptorMolecular biologyProtease-activated receptor 2
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Proteomic Analyses Reveal an Acidic Prime Side Specificity for the Astacin Metalloprotease Family Reflected by Physiological Substrates

2011

Astacins are secreted and membrane-bound metalloproteases with clear associations to many important pathological and physiological processes. Yet with only a few substrates described their biological roles are enigmatic. Moreover, the lack of knowledge of astacin cleavage site specificities hampers assay and drug development. Using PICS (proteomic identification of protease cleavage site specificity) and TAILS (terminal amine isotopic labeling of substrates) degradomics approaches >3000 cleavage sites were proteomically identified for five different astacins. Such broad coverage enables family-wide determination of specificities N- and C-terminal to the scissile peptide bond. Remarkably, me…

KeratinocytesModels MolecularProteomicsVascular Endothelial Growth Factor AProteasesmedicine.medical_treatmentProteolysisMolecular Sequence DataBiologyCleavage (embryo)BiochemistryCell LineSubstrate SpecificityAnalytical Chemistry03 medical and health sciencesTandem Mass SpectrometrymedicineHumansAmino Acid SequenceMolecular BiologyPeptide sequencePhylogeny030304 developmental biologyEnzyme Precursors0303 health sciencesProteaseStaining and LabelingEdman degradationmedicine.diagnostic_testResearch030302 biochemistry & molecular biologyTioproninMetalloendopeptidasesTerminal amine isotopic labeling of substratesRecombinant ProteinsKineticsBiochemistryProteolysisKallikreinsAstacinPeptidesSequence AlignmentChromatography LiquidMolecular &amp; Cellular Proteomics
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Inhibition Mechanism of SARS‐CoV‐2 Main Protease with Ketone‐Based Inhibitors Unveiled by Multiscale Simulations: Insights for Improved Designs**

2021

Abstract We present the results of classical and QM/MM simulations for the inhibition of SARS‐CoV‐2 3CL protease by a hydroxymethylketone inhibitor, PF‐00835231. In the noncovalent complex the carbonyl oxygen atom of the warhead is placed in the oxyanion hole formed by residues 143 to 145, while P1–P3 groups are accommodated in the active site with interactions similar to those observed for the peptide substrate. According to alchemical free energy calculations, the P1′ hydroxymethyl group also contributes to the binding free energy. Covalent inhibition of the enzyme is triggered by the proton transfer from Cys145 to His41. This step is followed by the nucleophilic attack of the Sγ atom on …

KetoneMolecular modelStereochemistrySubstituentMolecular Dynamics SimulationSARS‐CoV‐2 Inhibitors | Hot PaperCatalysisQM/MM3CL proteasechemistry.chemical_compoundCatalytic DomaininhibitorsHumansHydroxymethylProtease InhibitorsCoronavirus 3C ProteasesResearch Articleschemistry.chemical_classificationPF-00835231Binding SitesbiologySARS-CoV-2molecular modelingActive siteCOVID-19General ChemistryGeneral MedicineKetonesCOVID-19 Drug TreatmentKineticschemistryCovalent bondDrug Designbiology.proteinThermodynamicsOxyanion holeResearch ArticleAngewandte Chemie
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Peptidyl Vinyl Ketone Irreversible Inhibitors of Rhodesain: Modifications of the P2 Fragment.

2020

In this paper, we report the design, synthesis and biological investigation of a series of peptidyl vinyl ketones obtained by modifying the P2 fragment of previously reported highly potent inhibitors of rhodesain, the main cysteine protease of Trypanosoma brucei rhodesiense. Investigation of the structure-activity relationship led us to identify new rhodesain inhibitors endowed with an improved selectivity profile (a selectivity index of up to 22 000 towards the target enzyme), and/or an improved antitrypanosomal activity in the sub-micromolar range.

KetoneStereochemistryTrypanosoma brucei bruceiTrypanosoma bruceiCysteine Proteinase Inhibitors01 natural sciencesBiochemistrycathepsin LCathepsin LStructure-Activity RelationshipParasitic Sensitivity TestsDrug DiscoveryTrypanosoma bruceiGeneral Pharmacology Toxicology and PharmaceuticsPharmacologychemistry.chemical_classificationrhodesainbiologyDose-Response Relationship DrugMolecular Structure010405 organic chemistryOrganic ChemistryselectivityTrypanosoma brucei rhodesienseKetonesbiology.organism_classificationCysteine proteaseTrypanocidal Agents0104 chemical sciences010404 medicinal & biomolecular chemistryCysteine EndopeptidasesEnzymechemistrybiology.proteinMolecular MedicineMichael acceptorSelectivityPeptidesChemMedChem
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