Search results for "Endopeptidases"

showing 5 items of 285 documents

Synthesis and Molecular Modeling Studies of Derivatives of a Highly Potent Peptidomimetic Vinyl Ester as Falcipain-2 Inhibitors

2012

Herein we report the synthesis of a set of constrained peptidomimetics endowed with an electrophilic vinyl ester warhead and structurally related to a previously identified lead compound, a potent and irreversible inhibitor of falcipain-2 (FP-2). FP-2 is the main hemoglobinase of the malaria parasite P. falciparum. The new compounds were evaluated for their inhibition against FP-2, and the results were rationalized on the basis of docking experiments. These studies underscore the pivotal role of both the ester function at the P1' site and the trifluoromethyl group of the P3 side chain in determining the correct orientation of the Michael acceptor warhead in the catalytic site, and as a cons…

peptidomimeticdMolecular modelPeptidomimeticStereochemistryPlasmodium falciparumVinyl esterBiochemistrycysteine proteasesfalcipain-2 inhibitorsAntimalarialschemistry.chemical_compoundCatalytic DomainDrug DiscoverySide chainHumansEnzyme InhibitorsMalaria FalciparumGeneral Pharmacology Toxicology and PharmaceuticsPharmacologyTrifluoromethylOrganic Chemistrydocking studiescysteine proteases; peptidomimeticd; docking studies; falcipain-2 inhibitorsMolecular Docking SimulationCysteine EndopeptidaseschemistryDocking (molecular)Michael reactionMolecular MedicinePeptidomimeticsLead compoundChemMedChem
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Synthesis and biological evaluation of novel peptidomimetics as rhodesain inhibitors

2016

Novel rhodesain inhibitors were developed by combining an enantiomerically pure 3-bromoisoxazoline warhead with a 1,4-benzodiazepine scaffold as specific recognition moiety. All compounds were proven to inhibit rhodesain with Ki values in the low-micromolar range. Their activity towards rhodesain was found to be coupled to an in vitro antitrypanosomal activity, with IC50 values ranging from the mid-micromolar to a low-micromolar value for the most active rhodesain inhibitor (R,S,S)-3. All compounds showed a good selectivity against the target enzyme since all of them were proven to be poor inhibitors of human cathepsin L. Novel rhodesain inhibitors were developed by combining an enantiomeri…

rhodesainPharmacologychemistry.chemical_classificationCathepsinPeptidomimetic010405 organic chemistryChemistryPeptidomimeticProton Magnetic Resonance SpectroscopyenPeptidomimetics; rhodesain; trypanosomaGeneral Medicine01 natural sciencesCombinatorial chemistryIn vitro0104 chemical sciencesCysteine Endopeptidases010404 medicinal & biomolecular chemistryEnzymeDrug DiscoveryIc50 valuesMoietyPeptidomimeticsCarbon-13 Magnetic Resonance SpectroscopytrypanosomaBiological evaluationJournal of Enzyme Inhibition and Medicinal Chemistry
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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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Dipeptidyl Enoates As Potent Rhodesain Inhibitors That Display a Dual Mode of Action

2015

Dipeptidyl enoates were prepared through a high-yielding two-step synthetic route. They have a dipeptidic structure with a 4-oxoenoate moiety as a warhead with multiple reactive sites. Dipeptidyl enoates were screened against rhodesain and human cathepsins B and L, and were found to be potent and selective inhibitors of rhodesain. Among them (S,E)-ethyl 5-((S)-2-{[(benzyloxy)carbonyl]amino}-3-phenylpropanamido)-7-methyl-4-oxooct-2-enoate (6) was the most potent, with an IC50 value of 16.4 nm and kinact/Ki=1.6×106 m−1 s−1 against rhodesain. These dipeptidyl enoates display a reversible mode of inhibition at very low concentrations and an irreversible mode at higher concentrations. Inhibition…

trypanosomiasisStereochemistrysleeping sicknessCathepsin LDrug Evaluation PreclinicalChemistry Techniques SyntheticInhibition kineticsCysteine Proteinase InhibitorsBiochemistryCathepsin BInhibitory Concentration 50Structure-Activity RelationshipinhibitorsDrug DiscoveryHumansMoietyMolecular Targeted TherapyGeneral Pharmacology Toxicology and PharmaceuticsIC50Volume concentrationrhodesainPharmacologyChemistryOrganic ChemistryDual modeDipeptidesTrypanocidal AgentsCombinatorial chemistryMolecular Docking SimulationCysteine EndopeptidasesKineticsdipeptidyl enoatesTrypanosomiasis AfricanDocking (molecular)Molecular MedicineCysteine thiolateChemMedChem
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Conformational Dynamics of the Dengue Virus Protease Revealed by Fluorescence Correlation and Single-Molecule FRET Studies.

2021

The dengue virus protease (DENV-PR) represents an attractive target for counteracting DENV infections. It is generally assumed that DENV-PR can exist in an open and a closed conformation and that active site directed ligands stabilize the closed state. While crystal structures of both the open and the closed conformation were successfully resolved, information about the prevalence of these conformations in solution remains elusive. Herein, we address the question of whether there is an equilibrium between different conformations in solution which can be influenced by addition of a competitive inhibitor. To this end, DENV-PR was statistically labeled by two dye molecules constituting a FRET …

virusesFluorescence correlation spectroscopyCrystal structureDengue virusViral Nonstructural Proteins010402 general chemistrymedicine.disease_cause01 natural sciencesCatalytic Domain0103 physical sciencesMaterials ChemistrymedicineFluorescence Resonance Energy TransferMoleculePhysical and Theoretical Chemistry010304 chemical physicsbiologyChemistrySerine EndopeptidasesActive siteSingle-molecule FRETDengue VirusFluorescence0104 chemical sciencesSurfaces Coatings and FilmsFörster resonance energy transferbiology.proteinBiophysicsThe journal of physical chemistry. B
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