Search results for "Molecular Docking"

showing 10 items of 186 documents

Identification of potential inhibitors targeting BRAF-V600E mutant melanoma cells.

2020

Models MolecularProto-Oncogene Proteins B-rafProtein ConformationMutantMutation MissenseDermatologyInhibitory Concentration 50Structure-Activity RelationshipCell Line TumormedicineHumansPoint MutationMolecular Targeted TherapyPrecision MedicineMelanomaProtein Kinase InhibitorsDose-Response Relationship Drugbusiness.industryMelanomaDrug Repositioningmedicine.diseaseNeoplasm ProteinsBRAF V600EMolecular Docking SimulationAmino Acid SubstitutionDrug DesignCancer researchIdentification (biology)Drug Screening Assays AntitumorbusinessJournal of the American Academy of Dermatology
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IKK-β inhibitors: An analysis of drug–receptor interaction by using Molecular Docking and Pharmacophore 3D-QSAR approaches

2010

Abstract The IKK kinases family represents a thrilling area of research because of its importance in regulating the activity of NF-kB transcription factors. The discovery of the central role played by IKK-β in the activation of transcription in response to apoptotic or inflammatory stimuli allowed to considerate its modulation as a promising tool for the treatment of chronic inflammation and cancer. To date, several IKK-β inhibitors have been discovered and tested. In this work, an analysis of the interactions between different classes of inhibitors and their biological target was performed, through the application of Molecular Docking and Pharmacophore/3D-QSAR approaches to a set of 141 in…

Models MolecularQuantitative structure–activity relationshipReceptors DrugMolecular Sequence DataQuantitative Structure-Activity RelationshipIκB kinaseComputational biologyPharmacologyBiologyMaterials ChemistryHumansAmino Acid SequenceNF-kBHomology modelingPhysical and Theoretical ChemistryProtein Kinase InhibitorsTranscription factorSpectroscopyIKK-betaIKK-beta inhibitors Molecular Docking Pharmacophore 3D-QSAR approachesBinding SitesPharmacophoreKinaseHomology modelingSettore CHIM/08 - Chimica FarmaceuticaComputer Graphics and Computer-Aided DesignI-kappa B KinaseMolecular DockingStructural Homology ProteinBiological targetDrug receptorPharmacophoreJournal of Molecular Graphics and Modelling
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N-(INDAZOLYL)BENZAMIDO DERIVATIVES AS CDK1 INHIBITORS: DESIGN, SYNTHESIS, BIOLOGICAL ACTIVITY, AND MOLECULAR DOCKING STUDIES

2009

A series of N-1H-indazole-1-carboxamides has been synthesized and their effects on both CDK1/cyclin B and the K-562 (human chronic myelogenus leukemia) cell line were evaluated. Using a computational model, we have observed that all the most active compounds 9e, f, i-n exhibited the same binding mode of purvanalol A in the ATP-binding cleft. Although they were able to moderately inhibit the leukemic cell line K-562 and to show inhibitory activity against the Cdc2-Cyclin B kinase in the low micromolar range, they turned out to be non-cytotoxic against HuDe (IZSL) primary cell cultures from human derm. These preliminary results are quite encouraging in view of the low toxicity demonstrated by…

Models MolecularStereochemistryCyclin BPharmaceutical ScienceAntineoplastic AgentsCyclin BStructure-Activity RelationshipCDC2 Protein KinaseDrug DiscoveryHumansStructure–activity relationshipCell ProliferationCyclin-dependent kinase 1Binding SitesbiologyCell growthChemistryImidazolesN-(1H-indazolyl)benzamides 1H-indazole-3-carboxamides CDK1 Molecular dockingBiological activitySettore CHIM/08 - Chimica FarmaceuticaBiochemistryDocking (molecular)Cell cultureDrug DesignBenzamidesbiology.proteinDrug Screening Assays AntitumorK562 CellsCDC2 Protein KinaseProtein Binding
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Inside the Hsp90 inhibitors binding mode through induced fit docking

2009

Abstract During the last few decades, the development of new anticancer strategies had to face the instability of many tumors, occurring when the genetic plasticity of cells produces new drug-resistant cancers. It has been shown that a chaperone protein, heat shock protein 90 (Hsp90), is one of the fundamental factors involved in the cell response to stresses, and its role in many biochemical pathways has been demonstrated. Thus, the inhibition of Hsp90 represents a new target of antitumor therapy, since it may influence many specific signaling pathways. The natural antibiotic Geldanamycin is the first Hsp90 inhibitor that has been identified. Nevertheless, more potent and water-soluble sma…

Models MolecularStereochemistryLactams MacrocyclicMolecular Sequence DataComputational biologyCrystallography X-RayLigandsHsp90 inhibitorchemistry.chemical_compoundAdenosine TriphosphateHeat shock proteinCatalytic DomainMaterials ChemistryBenzoquinonesAmino Acid SequenceHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistrySpectroscopyInduced fitBinding SitesbiologyMolecular StructureHeat shock proteinDrug discoveryActive siteGeldanamycinRadicicolComputer Graphics and Computer-Aided DesignSmall moleculeHsp90Settore CHIM/08 - Chimica FarmaceuticachemistryDocking (molecular)Molecular dockingbiology.proteinGeldanamicynSequence AlignmentProtein Binding
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Development of new Coumarin-based profluorescent substrates for human cytochrome P450 enzymes

2018

Cytochrome P450 (CYP) enzymes constitute an essential xenobiotic metabolizing system that regulates the elimination of lipophilic compounds from the body. Convenient and affordable assays for CYP enzymes are important for assessing these metabolic pathways.In this study, 10 novel profluorescent coumarin derivatives with various substitutions at carbons 3, 6 and 7 were developed. Molecular modeling indicated that 3-phenylcoumarin offers an excellent scaffold for the development of selective substrate compounds for various human CYP forms, as they could be metabolized to fluorescent 7-hydroxycoumarin derivatives. Oxidation of profluorescent coumarin derivatives to fluorescent metabolites by 1…

Models MolecularentsyymitoxidationHealth Toxicology and MutagenesisToxicology030226 pharmacology & pharmacyBiochemistrycoumarinFluorescence03 medical and health scienceschemistry.chemical_compound0302 clinical medicineCytochrome P-450 Enzyme SystemCoumarinsCYPenzyme kineticsderivativeCytochrome P-450 Enzyme InhibitorsHumansheterocyclic compoundsEnzyme kineticskumariiniCYP2A6ta317Pharmacologychemistry.chemical_classificationBenzoflavonesbiologyChemistryCYP1A2fluoresenssiCytochrome P450substraatit (kemia)General MedicineCoumarindrug metabolismMolecular Docking SimulationMetabolic pathwayKineticsEnzymeBiochemistrylääkekemia030220 oncology & carcinogenesisInactivation Metabolicbiology.proteinMicrosomes LiverOxidation-ReductionDrug metabolism
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Design and Synthesis of Novel 1,3-Thiazole and 2-Hydrazinyl-1,3-Thiazole Derivatives as Anti-

2019

In the context of there being a limited number of clinically approved drugs for the treatment of Candida sp.-based infections, along with the rapid development of resistance to the existing antifungals, two novel series of 4-phenyl-1,3-thiazole and 2-hydrazinyl-4-phenyl-1,3-thiazole derivatives were synthesized and tested in vitro for their anti-Candida potential. Two compounds (7a and 7e) showed promising inhibitory activity against the pathogenic C. albicans strain, exhibiting substantially lower MIC values (7.81 μg/mL and 3.9 μg/mL, respectively) as compared with the reference drug fluconazole (15.62 μg/mL). Their anti-Candida activity is also supported by molecular docking studies, usin…

Molecular Docking Simulation13-thiazoleStructure-Activity RelationshipAntifungal Agentsbovine serum albuminfluorescence quenchingSerum Albumin Bovineanti-Candidamolecular dockingArticleCandidaMolecules (Basel, Switzerland)
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Suitability ofMMGBSAfor the selection of correct ligand binding modes from docking results

2018

The estimation of the correct binding mode and affinity of a ligand into a target protein using computational methods is challenging. However, docking can introduce poses from which the correct binding mode could be identified using other methods. Here, we analyzed the reliability of binding energy estimation using the molecular mechanics-generalized Born surface area (MMGBSA) method without and with energy minimization to identify the likely ligand binding modes within docking results. MMGBSA workflow (a) outperformed docking in recognizing the correct binding modes of androgen receptor ligands and (b) improved the correlation coefficient of computational and experimental results of rescor…

Molecular modelBinding energyta3111LigandsEnergy minimization01 natural sciencesBiochemistrylääkesuunnitteluSubstrate SpecificityCytochrome P-450 CYP2A6Free energy perturbationCoumarinsDrug DiscoveryHumansta317PharmacologyBinding Sitesmolecular modeling010405 organic chemistryChemistryDrug discoveryOrganic Chemistryta1182liganditreceptor and ligandslaskennallinen kemiaLigand (biochemistry)Protein Structure Tertiary0104 chemical sciencesMolecular Docking Simulation010404 medicinal & biomolecular chemistryDocking (molecular)structure based drug-designThermodynamicsMolecular MedicineproteiinitTarget proteinBiological systemProtein BindingChemical Biology & Drug Design
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New potent antibacterials against Gram-positive multiresistant pathogens: effects of side chain modification and chirality in linezolid-like 1,2,4-ox…

2014

The effects of side chain modification and chirality in linezolid-like 1,2,4-oxadiazoles have been studied to design new potent antibacterials against Gram-positive multidrug-resistant pathogens. The adopted strategy involved a molecular modelling approach, the synthesis and biological evaluation of new designed compounds, enantiomers separation and absolute configuration assignment. Experimental determination of the antibacterial activity of the designed (S)-1-((3-(4-(3-methyl-1,2,4-oxadiazol-5- yl)phenyl)-oxazolidin-2-one-5-yl)methyl)-3-methylthiourea and (S)-1-((3-(3-fluoro-4-(3-methyl-1,2,4- oxadiazol-5-yl)phenyl)-oxazolidin-2-one-5-yl)methyl)-3-methylthiourea against multidrug resistan…

Multidrug-resistant bacteriaClinical BiochemistryAntibioticsDrug ResistanceMolecular ConformationPharmaceutical ScienceBiochemistrychemistry.chemical_compoundAntibioticsDrug Resistance Multiple BacterialDrug DiscoveryAcetamidesSide chainOxadiazolesAbsolute configurationBacterialStereoisomerismHep G2 CellsBIO/10 - BIOCHIMICA23SAnti-Bacterial AgentsMolecular Docking SimulationRNA Ribosomal 23SDrug design Linezolid Antibiotics Multidrug-resistant bacteria EnantiomersMolecular MedicineAntibacterial activityMultipleMethicillin-Resistant Staphylococcus aureusStaphylococcus aureusmedicine.drug_classStereochemistryCell SurvivalMicrobial Sensitivity TestsGram-Positive BacteriaDrug designmedicineHumansMolecular BiologyOxazolidinonesRibosomalBinding SitesOrganic ChemistryAntibioticLinezolidSettore CHIM/06 - Chimica OrganicaSettore CHIM/08 - Chimica FarmaceuticaMultiple drug resistancechemistryEnantiomersMED/07 - MICROBIOLOGIA E MICROBIOLOGIA CLINICALinezolidRNANucleic Acid ConformationEnantiomerChirality (chemistry)Bioorganicmedicinal chemistry
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The crystal structure of a 250-kDa heterotetrameric particle explains inhibition of sheddase meprin β by endogenous fetuin-B

2021

Meprin β (Mβ) is a multidomain type-I membrane metallopeptidase that sheds membrane-anchored substrates, releasing their soluble forms. Fetuin-B (FB) is its only known endogenous protein inhibitor. Herein, we analyzed the interaction between the ectodomain of Mβ (MβΔC) and FB, which stabilizes the enzyme and inhibits it with subnanomolar affinity. The MβΔC:FB crystal structure reveals a ∼250-kDa, ∼160-Å polyglycosylated heterotetrameric particle with a remarkable glycan structure. Two FB moieties insert like wedges through a “CPDCP trunk” and two hairpins into the respective peptidase catalytic domains, blocking the catalytic zinc ions through an “aspartate switch” mechanism. Uniquely, the …

Multiprotein complexMetallopeptidaseCleavage (embryo)Cell LineMiceProtein structureAnimalsHumansEctoprotein sheddingProtease InhibitorsInhibitionBinding SitesMultidisciplinarybiologyChemistryMetallopeptidaseMetalloendopeptidasesActive siteBiological SciencesSheddaseFetuin-BLepidopteraMolecular Docking SimulationTransmembrane domainEctodomainbiology.proteinBiophysicsProtein structureMultiprotein complexAlzheimer’s diseaseProtein Binding
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Deciphering the Potential of Pre and Pro-Vitamin D of Mushrooms against Mpro and PLpro Proteases of COVID-19: An In Silico Approach

2022

Vitamin D’s role in combating the SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2), the virus causing COVID-19, has been established in unveiling viable inhibitors of COVID-19. The current study investigated the role of pre and pro-vitamin D bioactives from edible mushrooms against Mpro and PLpro proteases of SARS-CoV-2 by computational experiments. The bioactives of mushrooms, specifically ergosterol (provitamin D2), 7-dehydrocholesterol (provitamin-D3), 22,23-dihydroergocalciferol (provitamin-D4), cholecalciferol (vitamin-D3), and ergocalciferol (vitamin D2) were screened against Mpro and PLpro. Molecular docking analyses of the generated bioactive protease complexes unr…

Pharmaceutical Scienceedible mushroomsMolecular Dynamics SimulationViral Nonstructural ProteinsAnalytical Chemistrypro-vitamin-DErgosterolDrug DiscoveryEndopeptidasespre-vitamin-DHumansProtease InhibitorsPhysical and Theoretical ChemistryVitamin DSARS-CoV-2Organic ChemistryProvitaminsin-silico studiesSettore CHIM/08 - Chimica FarmaceuticaCOVID-19 Drug TreatmentMolecular Docking SimulationChemistry (miscellaneous)Molecular MedicineAgaricalesedible mushrooms; SARS-CoV-2; pre-vitamin-D; pro-vitamin-D; in-silico studiesPeptide HydrolasesMolecules; Volume 27; Issue 17; Pages: 5620
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