Search results for "3C protease"

showing 10 items of 12 documents

In silico drug discovery of major metabolites from spices as SARS-CoV-2 main protease inhibitors

2020

Coronavirus Disease 2019 (COVID-19) is an infectious illness caused by Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), originally identified in Wuhan, China (December 2019) and has since expanded into a pandemic. Here, we investigate metabolites present in several common spices as possible inhibitors of COVID-19. Specifically, 32 compounds isolated from 14 cooking seasonings were examined as inhibitors for SARS-CoV-2 main protease (Mpro), which is required for viral multiplication. Using a drug discovery approach to identify possible antiviral leads, in silico molecular docking studies were performed. Docking calculations revealed a high potency of salvianolic acid A and curcu…

0301 basic medicineCurcuminIn silicomedicine.medical_treatmentPneumonia ViralHealth InformaticsMolecular dynamicsMolecular Dynamics SimulationViral Nonstructural ProteinsArticleSARS-CoV-2 main proteaseBetacoronavirus03 medical and health scienceschemistry.chemical_compoundCaffeic Acids0302 clinical medicineDrug DiscoverymedicineHumansProtease InhibitorsSpicesPandemicsCoronavirus 3C Proteaseschemistry.chemical_classificationNatural productProteaseSARS-CoV-2Secondary metabolitesCOVID-19LopinavirAmino acidComputer Science ApplicationsMolecular Docking SimulationCysteine Endopeptidases030104 developmental biologyEnzymechemistryBiochemistryDocking (molecular)Molecular dockingLactatesCurcuminThermodynamicsCoronavirus Infections030217 neurology & neurosurgerymedicine.drugComputers in Biology and Medicine
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The dimer-monomer equilibrium of SARS-CoV-2 main protease is affected by small molecule inhibitors

2021

AbstractThe maturation of coronavirus SARS-CoV-2, which is the etiological agent at the origin of the COVID-19 pandemic, requires a main protease Mpro to cleave the virus-encoded polyproteins. Despite a wealth of experimental information already available, there is wide disagreement about the Mpro monomer-dimer equilibrium dissociation constant. Since the functional unit of Mpro is a homodimer, the detailed knowledge of the thermodynamics of this equilibrium is a key piece of information for possible therapeutic intervention, with small molecules interfering with dimerization being potential broad-spectrum antiviral drug leads. In the present study, we exploit Small Angle X-ray Scattering (…

0301 basic medicineMolecular biologyProtein ConformationSciencemedicine.medical_treatmentDimerBiophysicsPlasma protein binding010402 general chemistryAntiviral Agents01 natural sciencesArticleDissociation (chemistry)03 medical and health scienceschemistry.chemical_compoundProtein structureX-Ray DiffractionDrug DiscoverymedicineHumansProtease InhibitorsCoronavirus 3C ProteasesVirtual screeningMultidisciplinaryProteaseSARS-CoV-2ChemistryQSARS-CoV-2 main protease Mpro enzymatic activity inhibition Small Angle X-ray Scattering small inhibitors virtual screeningRCOVID-19Computational BiologySmall moleculeComputational biology and bioinformatics0104 chemical sciencesMolecular Docking SimulationDissociation constant030104 developmental biologyBiophysicsMedicineThermodynamicsDimerizationProtein Binding
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Famotidine inhibits toll-like receptor 3-mediated inflammatory signaling in SARS-CoV-2 infection

2021

Apart from prevention using vaccinations, the management options for COVID-19 remain limited. In retrospective cohort studies, use of famotidine, a specific oral H2 receptor antagonist (antihistamine), has been associated with reduced risk of intubation and death in patients hospitalized with COVID-19. In a case series, nonhospitalized patients with COVID-19 experienced rapid symptom resolution after taking famotidine, but the molecular basis of these observations remains elusive. Here we show using biochemical, cellular, and functional assays that famotidine has no effect on viral replication or viral protease activity. However, famotidine can affect histamine-induced signaling processes i…

0301 basic medicinemedicine.medical_treatmentPharmacologyVirus ReplicationBiochemistrychemistry.chemical_compoundChemokine CCL2Coronavirus 3C ProteasesResearch ArticlesToll-like receptorbiologyNF-kappa BFamotidineMolecular Docking SimulationCytokine release syndromeCytokinemedicine.symptomSignal transductionHistaminemedicine.drugProtein BindingSignal TransductionHistamine AntagonistsInflammation03 medical and health sciencesToll-like receptormedicineHumansInterleukin 6Molecular BiologyBinding Sites030102 biochemistry & molecular biologybusiness.industryInterleukin-6SARS-CoV-2Cell Biologymedicine.diseasehistamineToll-Like Receptor 3Famotidine030104 developmental biologychemistryA549 CellsSARS-CoV2biology.proteinanti-viral signalingInterferon Regulatory Factor-3Caco-2 CellsbusinessHeLa Cells
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Structure‐Activity Relationships of Benzamides and Isoindolines Designed as SARS‐CoV Protease Inhibitors Effective against SARS‐CoV‐2

2020

Abstract Inhibition of coronavirus (CoV)‐encoded papain‐like cysteine proteases (PLpro) represents an attractive strategy to treat infections by these important human pathogens. Herein we report on structure‐activity relationships (SAR) of the noncovalent active‐site directed inhibitor (R)‐5‐amino‐2‐methyl‐N‐(1‐(naphthalen‐1‐yl)ethyl) benzamide (2 b), which is known to bind into the S3 and S4 pockets of the SARS‐CoV PLpro. Moreover, we report the discovery of isoindolines as a new class of potent PLpro inhibitors. The studies also provide a deeper understanding of the binding modes of this inhibitor class. Importantly, the inhibitors were also confirmed to inhibit SARS‐CoV‐2 replication in …

Computational chemistryProteases2019-20 coronavirus outbreakCoronavirus disease 2019 (COVID-19)medicine.medical_treatmentSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)virusesStructure-activity relationshipsCysteine Proteinase InhibitorsIsoindolesCrystallography X-RayVirus Replicationmedicine.disease_causeAntiviral Agents01 natural sciencesBiochemistryDrug designStructure-Activity Relationshipchemistry.chemical_compoundCatalytic DomainChlorocebus aethiopsDrug DiscoverymedicineAnimalsddc:610General Pharmacology Toxicology and PharmaceuticsBenzamideVero CellsCoronavirus 3C ProteasesCoronavirusPharmacologyProteaseMolecular StructureFull PaperSARS-CoV-2010405 organic chemistryOrganic ChemistryFull PapersProtease inhibitors0104 chemical sciencesMolecular Docking Simulation010404 medicinal & biomolecular chemistrychemistryBiochemistryBenzamidesddc:540Molecular MedicineProtein BindingCysteine
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Microscopic interactions between ivermectin and key human and viral proteins involved in SARS-CoV-2 infection

2021

The identification of chemical compounds able to bind specific sites of the human/viral proteins involved in the SARS-CoV-2 infection cycle is a prerequisite to design effective antiviral drugs. Here we conduct a molecular dynamics study with the aim to assess the interactions of ivermectin, an antiparasitic drug with broad-spectrum antiviral activity, with the human Angiotensin-Converting Enzyme 2 (ACE2), the viral 3CLpro and PLpro proteases, and the viral SARS Unique Domain (SUD). The drug/target interactions have been characterized in silico by describing the nature of the non-covalent interactions found and by measuring the extent of their time duration along the MD simulation. Results …

DrugProteasesIn silicomedia_common.quotation_subjectProtein domainCoronavirus Papain-Like ProteasesGeneral Physics and AstronomyPlasma protein bindingBiologyAntiviral AgentsivermectinProtein DomainsMolecular dynamics simulationHumansPhysical and Theoretical ChemistryBinding siteCoronavirus 3C Proteasesmedia_commonchemistry.chemical_classificationSARS Unique DomainBinding SitesSARS-CoV-2SARS-CoV-2 infectionRNAHydrogen BondingVirologyG-QuadruplexesMolecular Docking SimulationEnzymechemistrySettore CHIM/03 - Chimica Generale E InorganicaRNAAngiotensin-Converting Enzyme 2Hydrophobic and Hydrophilic InteractionsProtein BindingPhysical Chemistry Chemical Physics
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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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New Tetromycin Derivatives with Anti-Trypanosomal and Protease Inhibitory Activities

2011

Four new tetromycin derivatives, tetromycins 1-4 and a previously known one, tetromycin B (5) were isolated from Streptomyces axinellae Pol001(T) cultivated from the Mediterranean sponge Axinella polypoides. Structures were assigned using extensive 1D and 2D NMR spectroscopy as well as HRESIMS analysis. The compounds were tested for antiparasitic activities against Leishmania major and Trypanosoma brucei, and for protease inhibition against several cysteine proteases such as falcipain, rhodesain, cathepsin L, cathepsin B, and viral proteases SARS-CoV M(pro), and PL(pro). The compounds showed antiparasitic activities against T. brucei and time-dependent inhibition of cathepsin L-like proteas…

Magnetic Resonance Spectroscopyanti-trypanosomalmedicine.medical_treatmentCathepsin LStreptomyces axinellaePharmaceutical ScienceCathepsin BCathepsin BCathepsin LCathepsin ODrug DiscoveryPharmacology Toxicology and Pharmaceutics (miscellaneous)lcsh:QH301-705.5Coronavirus 3C ProteasesLeishmania major0303 health sciencesbiology030302 biochemistry & molecular biologytetromycin; anti-trypanosomal; protease inhibition; <em>Streptomyces axinellae</em>; marine spongeTrypanocidal AgentsStreptomycesCysteine EndopeptidasesBiochemistrySevere acute respiratory syndrome-related coronavirusStreptomyces axinellaetetromycinBiologiemarine spongeddc:547ProteasesTrypanosoma brucei bruceiAntiprotozoal AgentsTrypanosoma bruceiHeterocyclic Compounds 4 or More RingsArticle03 medical and health sciencesViral ProteinsAxinellaparasitic diseasesmedicineAnimalsProtease Inhibitorsddc:610protease inhibition ; anti-trypanosomal ; Streptomyces axinellae ; tetromycin ; marine sponge030304 developmental biologyCathepsinProteasebiology.organism_classificationprotease inhibitionlcsh:Biology (General)biology.protein
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In Silico Insights into the SARS CoV-2 Main Protease Suggest NADH Endogenous Defences in the Control of the Pandemic Coronavirus Infection

2020

COVID-19 is a pandemic health emergency faced by the entire world. The clinical treatment of the severe acute respiratory syndrome (SARS) CoV-2 is currently based on the experimental administration of HIV antiviral drugs, such as lopinavir, ritonavir, and remdesivir (a nucleotide analogue used for Ebola infection). This work proposes a repurposing process using a database containing approximately 8000 known drugs in synergy structure- and ligand-based studies by means of the molecular docking and descriptor-based protocol. The proposed in silico findings identified new potential SARS CoV-2 main protease (MPRO) inhibitors that fit in the catalytic binding site of SARS CoV-2 MPRO. Several sel…

Models Molecular0301 basic medicineAgingmedicine.medical_treatmentcoronaviruslcsh:QR1-502Viral Nonstructural Proteinsmedicine.disease_causelcsh:Microbiology0302 clinical medicineSettore BIO/10 - BiochimicaCoronavirus 3C ProteasesCoronavirusvirus diseasesLopinavirHypothesisMolecular Docking SimulationCysteine EndopeptidasesDrug repositioningInfectious Diseases030220 oncology & carcinogenesisCoronavirus InfectionsOxidation-Reductionmedicine.drugDNA damageIn silicoPneumonia ViralBiologyAntiviral AgentsHIV-proteaseBetacoronavirus03 medical and health sciencesSARS-CoV-2 main proteaseVirologymedicineHumansComputer SimulationProtease InhibitorsPandemicsBinding SitesProteaseSARS-CoV-2Drug RepositioningCOVID-19HIV Protease InhibitorsDRUDIT web servicemolecular dockingNADbiology.organism_classificationVirologySettore CHIM/08 - Chimica FarmaceuticaCOVID-19 Drug Treatmentcoronaviru030104 developmental biologyNADHRitonavirBetacoronavirusDNA Damage
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Evidence for substrate binding-induced zwitterion formation in the catalytic Cys-His dyad of the SARS-CoV main protease.

2014

The coronavirus main protease (M(pro)) represents an attractive drug target for antiviral therapy of coronavirus (CoV) infections, including severe acute respiratory syndrome (SARS). The SARS-CoV M(pro) and related CoV proteases have several distinct features, such as an uncharged Cys-His catalytic dyad embedded in a chymotrypsin-like protease fold, that clearly separate these enzymes from archetypical cysteine proteases. To further characterize the catalytic system of CoV main proteases and to obtain information about improved inhibitors, we performed comprehensive simulations of the proton-transfer reactions in the SARS-CoV M(pro) active site that lead to the Cys(-)/His(+) zwitterionic st…

Models MolecularProteasesStereochemistryvirusesmedicine.medical_treatmentEntropyStatic ElectricityMolecular Dynamics Simulationmedicine.disease_causeBiochemistrySubstrate Specificitychemistry.chemical_compoundViral ProteinsCatalytic DomainmedicineHistidineCysteineHistidineCoronavirus 3C ProteasesCoronaviruschemistry.chemical_classificationProteasebiologyChemistryvirus diseasesActive siteCysteine EndopeptidasesEnzymeBiochemistryZwitterionbiology.proteinCysteineBiochemistry
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Enteroviruses and coronaviruses: similarities and therapeutic targets

2021

ABSTRACT Introduction: Enteroviruses are common viruses causing a huge number of acute and chronic infections and producing towering economic costs. Similarly, coronaviruses cause seasonal mild infections, epidemics, and even pandemics and can lead to severe respiratory symptoms. It is important to develop broadly acting antiviral molecules to efficiently tackle the infections caused by thes. Areas covered: This review illuminates the differences and similarities between enteroviruses and coronaviruses and examines the most appealing therapeutic targets to combat both virus groups. Publications of both virus groups and deposited structures discovered through PubMed to March 2021 for viral p…

ProteasesPolyproteinsvirusesmedicine.medical_treatmentClinical BiochemistrycoronavirusReviewSARS-COV-2Biologymedicine.disease_causeAntiviral Agents3C proteaseVirusSubstrate Specificity03 medical and health sciencesDrug DiscoveryPandemicmedicineAnimalsHumansVirus classificationEnterovirus030304 developmental biologyCoronavirusPharmacology0303 health sciencesProtease030306 microbiologyCOVID-19Virology3. Good healthCysteine Endopeptidasesmain proteaseMolecular MedicineEnterovirusResearch ArticleExpert Opinion on Therapeutic Targets
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