Search results for "Aminoacyltransferases"

showing 10 items of 10 documents

Targeting Bacterial Sortase A with Covalent Inhibitors: 27 New Starting Points for Structure-Based Hit-to-Lead Optimization.

2019

Because of its essential role as a bacterial virulence factor, enzyme sortase A (SrtA) has become an attractive target for the development of new antivirulence drugs against Gram-positive infections. Here we describe 27 compounds identified as covalent inhibitors of

0301 basic medicineStaphylococcus aureusMagnetic Resonance SpectroscopyAntivirulenceVirulence Factors030106 microbiologySmall Molecule Libraries03 medical and health sciencesMiceBacterial ProteinsCatalytic DomainDrug DiscoveryAnimalschemistry.chemical_classificationBinding SitesChemistryHit to leadFibroblastsAminoacyltransferasesAnti-Bacterial AgentsMolecular Docking SimulationCysteine Endopeptidases030104 developmental biologyInfectious DiseasesEnzymeBiochemistryCovalent bondSortase ABacterial virulenceNIH 3T3 CellsStructure basedACS infectious diseases
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1,2,4-Oxadiazole topsentin analogs as staphylococcal biofilm inhibitors targeting the bacterial transpeptidase sortase A

2020

The inhibition or prevention of biofilm formation represents an emerging strategy in the war against antibiotic resistance, interfering with key players in bacterial virulence. This approach includes the inhibition of the catalytic activity of transpeptidase sortase A (Srt A), a membrane enzyme responsible for covalently attaching a wide variety of adhesive matrix molecules to the peptidoglycan cell wall in Gram-positive strains. A new series of seventeen 1,2,4-oxadiazole derivatives was efficiently synthesized and screened as potential new anti-virulence agents. The ability of inhibiting biofilm formation was evaluated against both Gram-positive and Gram-negative pathogens. Remarkably, all…

Indoles124-Oxadiazoles Antibiofilm activity Sortase A inhibitors Anti-virulence agents Marine alkaloids Topsentin analogs01 natural scienceslaw.inventionchemistry.chemical_compoundMarine alkaloidslawDrug DiscoveryPathogenchemistry.chemical_classificationOxadiazoles0303 health sciencesChemistry4-OxadiazolesImidazolesGeneral MedicineStaphylococcal InfectionsAminoacyltransferasesAnti-Bacterial AgentsCysteine EndopeptidasesAnti-virulence agentsBiochemistrySortase AAntibiofilm activityPseudomonas aeruginosaTopsentin analogsRecombinant DNA124-Oxadiazoles; Anti-virulence agents; Antibiofilm activity; Marine alkaloids; Sortase A inhibitors; Topsentin analogsStaphylococcus aureus12Sortase A inhibitorsCell LineCell wall03 medical and health sciencesAntibiotic resistanceBacterial Proteins124-OxadiazolesHumansPseudomonas Infections030304 developmental biologyPharmacology010405 organic chemistryOrganic ChemistryBiofilmSettore CHIM/08 - Chimica Farmaceutica0104 chemical sciencesEnzymeBiofilmsPeptidoglycan
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Sortase A Inhibitors: Recent Advances and Future Perspectives

2015

Here, we describe the most promising small synthetic organic compounds that act as potent Sortase A inhibitors and cater the potential to be developed as antivirulence drugs. Sortase A is a polypeptide of 206 amino acids, which catalyzes two sequential reactions: (i) thioesterification and (ii) transpeptidation. Sortase A is involved in the process of bacterial adhesion by anchoring LPXTG-containing proteins to lipid II. Sortase A inhibitors do not affect bacterial growth, but they restrain the virulence of pathogenic bacterial strains, thereby preventing infections caused by Staphylococcus aureus or other Gram-positive bacteria. The efficacy of the most promising inhibitors needs to be com…

Models MolecularStaphylococcus aureusRhodanineProtein ConformationVirulenceAdamantanemedicine.disease_causeStaphylococcal infectionsSettore BIO/19 - Microbiologia GeneraleBenzoatesBacterial AdhesionSortase A inhibitors review future perspectiveMicrobiologySmall Molecule LibrariesBacterial ProteinsIn vivoDrug DiscoveryNitrilesmedicineAnimalsHumansEnzyme Inhibitorschemistry.chemical_classificationLipid IIbiologyThionesStaphylococcal Infectionsbiology.organism_classificationmedicine.diseaseAminoacyltransferasesSettore CHIM/08 - Chimica FarmaceuticaAmino acidAnti-Bacterial AgentsCysteine EndopeptidasesThiazolesBiochemistrychemistryStaphylococcus aureusSortase AMolecular MedicineBacteriaCarbolines
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Evolution and functional differentiation of recently diverged phytochelatin synthase genes from Arundo donax L.

2019

Plant phytochelatin synthases undergo evolutionarily rapid functional differentiation after duplication, allowing fast and precise adjustment of metal detoxification capacity by modulation of both transcription and enzymatic activity.

Settore BIO/01 - BOTANICA GENERALE0106 biological sciences0301 basic medicineGene duplicationPhysiologyArabidopsisSaccharomyces cerevisiaePlant SciencePoaceae01 natural sciencesGenomeDivergenceEvolution Molecular03 medical and health sciencesGene Expression Regulation Plantcadmium; divergence; gene duplication; giant reed; phytochelatin synthase; phytochelatins; subfunctionalizationSubfunctionalizationPhytochelatinsArabidopsis thalianaAmino Acid SequenceGenePhylogenyPlant ProteinsGeneticsNatural selectionGiant reedbiologyArundo donaxAminoacyltransferasesPlants Genetically Modifiedbiology.organism_classificationResearch PapersPhenotype030104 developmental biologyPlant—Environment InteractionsSubfunctionalizationPhytochelatinMicroorganisms Genetically-ModifiedPhytochelatin synthaseSequence AlignmentCadmium010606 plant biology & botanyJournal of Experimental Botany
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Pyrrolomycins as antimicrobial agents. Microwave-assisted organic synthesis and insights into their antimicrobial mechanism of action

2019

Abstract New compounds able to counteract staphylococcal biofilm formation are needed. In this study we investigate the mechanism of action of pyrrolomycins, whose potential as antimicrobial agents has been demonstrated. We performed a new efficient and easy method to use microwave organic synthesis suitable for obtaining pyrrolomycins in good yields and in suitable amount for their in vitro in-depth investigation. We evaluate the inhibitory activity towards Sortase A (SrtA), a transpeptidase responsible for covalent anchoring in Gram-positive peptidoglycan of many surface proteins involved in adhesion and in biofilm formation. All compounds show a good inhibitory activity toward SrtA, havi…

Staphylococcus aureusClinical BiochemistryPharmaceutical ScienceMicrobial Sensitivity Testsmedicine.disease_causeSettore BIO/19 - Microbiologia Generale01 natural sciencesBiochemistrychemistry.chemical_compoundBacterial ProteinsDrug DiscoverymedicinePyrrolesEnzyme InhibitorsMicrowavesMolecular BiologyEnzyme Assays010405 organic chemistryChemistryOrganic ChemistryBiofilmN-Acetylmuramoyl-L-alanine AmidaseAntimicrobialAminoacyltransferasesAntimicrobial resistance Pyrrolomycins Sortase A Staphylococcus aureus In-silico docking studies MAOS Pharmacokinetics studies Murein hydrolase activitySettore CHIM/08 - Chimica Farmaceutica0104 chemical sciencesAnti-Bacterial AgentsMolecular Docking Simulation010404 medicinal & biomolecular chemistryCysteine EndopeptidasesBiochemistryMechanism of actionDocking (molecular)Staphylococcus aureusSettore CHIM/03 - Chimica Generale E InorganicaSortase ABiofilmsPseudomonas aeruginosaMolecular MedicineOrganic synthesisPeptidoglycanmedicine.symptom
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Discovery and structure-activity relationship studies of irreversible benzisothiazolinone-based inhibitors against Staphylococcus aureus sortase A tr…

2014

Gram-positive bacteria, in general, and staphylococci, in particular, are the widespread cause of nosocomial and community-acquired infections. The rapid evolvement of strains resistant to antibiotics currently in use is a serious challenge. Novel antimicrobial compounds have to be developed to fight these resistant bacteria, and sortase A, a bacterial cell wall enzyme, is a promising target for novel therapies. As a transpeptidase that covalently attaches various virulence factors to the cell surface, this enzyme plays a crucial role in the ability of bacteria to invade the host's tissues and to escape the immune response. In this study we have screened a small molecule library against rec…

Staphylococcus aureusClinical BiochemistryPharmaceutical ScienceVirulenceStaphylococcal infectionsmedicine.disease_causeBiochemistryBacterial cell structureMicrobiologyStructure-Activity RelationshipBacterial ProteinsSortaseDrug DiscoverymedicineFluorescence Resonance Energy TransferHumansEnzyme InhibitorsMolecular BiologybiologyChemistryOrganic ChemistryStaphylococcal InfectionsAntimicrobialmedicine.diseasebiology.organism_classificationAminoacyltransferasesHigh-Throughput Screening AssaysMolecular Docking SimulationCysteine EndopeptidasesThiazolesBiochemistryStaphylococcus aureusSortase AMolecular MedicineBacteriaBioorganicmedicinal chemistry
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Asymmetric Disulfanylbenzamides as Irreversible and Selective Inhibitors of Staphylococcus aureus Sortase A

2020

Abstract Staphylococcus aureus is one of the most frequent causes of nosocomial and community‐acquired infections, with drug‐resistant strains being responsible for tens of thousands of deaths per year. S. aureus sortase A inhibitors are designed to interfere with virulence determinants. We have identified disulfanylbenzamides as a new class of potent inhibitors against sortase A that act by covalent modification of the active‐site cysteine. A broad series of derivatives were synthesized to derive structure‐activity relationships (SAR). In vitro and in silico methods allowed the experimentally observed binding affinities and selectivities to be rationalized. The most active compounds were f…

Staphylococcus aureusmedicine.drug_classdrug designAntibioticsVirulenceMicrobial Sensitivity Testsmedicine.disease_cause01 natural sciencesBiochemistrybiofilmMicrobiology570 Life sciencesStructure-Activity RelationshipBacterial ProteinsAntibioticssortase ADrug DiscoverymedicineGeneral Pharmacology Toxicology and PharmaceuticsEnzyme InhibitorsCytotoxicityPharmacologyFull PaperDose-Response Relationship DrugMolecular Structure010405 organic chemistryChemistryOrganic ChemistryBiofilmFull PapersAminoacyltransferasesIn vitro0104 chemical sciencesAnti-Bacterial Agents010404 medicinal & biomolecular chemistryCysteine EndopeptidasesStaphylococcus aureusSortase Addc:540BenzamidesMolecular MedicineCysteine570 BiowissenschaftenChemmedchem
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Sortase A: An ideal target for anti-virulence drug development

2014

Sortase A is a membrane enzyme responsible for the anchoring of surface-exposed proteins to the cell wall envelope of Gram-positive bacteria. As a well-studied member of the sortase subfamily catalysing the cell wall anchoring of important virulence factors to the surface of staphylococci, enterococci and streptococci, sortase A plays a critical role in Gram-positive bacterial pathogenesis. It is thus considered a promising target for the development of new anti-infective drugs that aim to interfere with important Gram-positive virulence mechanisms, such as adhesion to host tissues, evasion of host defences, and bio fi lm formation. The additional properties of sortase A as an enzyme that i…

Virulence FactorsIn silicoVirulenceBiologyGram-Positive BacteriaAntimicrobial resistanceSettore BIO/19 - Microbiologia GeneraleMicrobiologyCell membraneAntibiotic resistanceGram-positive pathogenBacterial ProteinsSortaseDrug DiscoverymedicineVirulenceSortase ABiofilmAminoacyltransferasesSettore CHIM/08 - Chimica FarmaceuticaAntivirulence drugAnti-Bacterial AgentsCysteine EndopeptidasesInfectious Diseasesmedicine.anatomical_structureBiochemistryDrug developmentSortase A inhibitorSortase A
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Characterization and transcription studies of a phytochelatin synthase gene from the solitary tunicate Ciona intestinalis exposed to cadmium.

2014

The major thiol-containing molecules involved in controlling the level of intracellular ROS in eukaryotes, acting as a nonenzymatic detoxification system, are metallothioneins (MTs), glutathione (GSH) and phytochelatins (PCs). Both MTs and GSH are well-known in the animal kingdom. PC was considered a prerogative of the plant kingdom but, in 2001, a phytochelatin synthase (PCS) gene was described in the nematode Caenorhabditis elegans; additional genes encoding this enzyme were later described in the earthworm Eisenia fetida and in the parasitic nematode Schistosoma mansoni but scanty data are available, up to now, for Deuterostomes. Here, we describe the molecular characteristics and transc…

phytochelatin synthase; Ciona intestinalis; ascidians; cadmium; cell proliferationcadmiumHealth Toxicology and MutagenesisMolecular Sequence DataAquatic ScienceGene Expression Regulation Enzymologicphytochelatin synthaseTranscription (biology)BotanyGene OrderMetallothioneinAnimalsProliferation MarkerCiona intestinalisAmino Acid SequenceGenePhylogenybiologyCell growthGene Expression Profilingbiology.organism_classificationAminoacyltransferasesCell biologyCiona intestinalisascidiansGene expression profilingCionacell proliferationSequence AlignmentWater Pollutants ChemicalCadmiumAquatic toxicology (Amsterdam, Netherlands)
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Discovery of a new class of sortase a transpeptidase inhibitors to tackle gram-positive pathogens: 2-(2-phenylhydrazinylidene)alkanoic acids and rela…

2016

A FRET-based random screening assay was used to generate hit compounds as sortase A inhibitors that allowed us to identify ethyl 3-oxo-2-(2-phenylhydrazinylidene)butanoate as an example of a new class of sortase A inhibitors. Other analogues were generated by changing the ethoxycarbonyl function for a carboxy, cyano or amide group, or introducing substituents in the phenyl ring of the ester and acid derivatives. The most active derivative found was 3-oxo-2-(2-(3,4dichlorophenyl)hydrazinylidene)butanoic acid (2b), showing an IC50 value of 50 µM. For a preliminary assessment of their antivirulence properties the new derivatives were tested for their antibiofilm activity. The most active compo…

sortase A; biofilms; 2-(2-phenylhydrazinylidene)alkanoic acid derivatives; FRET0301 basic medicineStaphylococcus aureusStereochemistryPharmaceutical ScienceRelated derivativesmedicine.disease_causeSettore BIO/19 - Microbiologia Generale01 natural sciencesArticleAnalytical Chemistrylcsh:QD241-441Inhibitory Concentration 5003 medical and health scienceschemistry.chemical_compound2-(2-phenylhydrazinylidene)alkanoic acid derivativeAnti-Infective AgentsBacterial Proteinslcsh:Organic chemistryStaphylococcus epidermidisAmideDrug DiscoveryStaphylococcus epidermidismedicineEnzyme InhibitorsPhysical and Theoretical ChemistryIC50Grambiology010405 organic chemistryChemistryBiofilmSortase AOrganic ChemistryBiofilmAminoacyltransferasesbiology.organism_classificationSettore CHIM/08 - Chimica Farmaceutica2-(2-phenylhydrazinylidene)alkanoic acid derivativesPhenylhydrazines0104 chemical sciencesCysteine Endopeptidases030104 developmental biologyChemistry (miscellaneous)Staphylococcus aureusSortase AFRETMolecular Medicinebiofilms
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