Search results for "Models"

showing 10 items of 8211 documents

The discovery of novel antitrypanosomal 4-phenyl-6-(pyridin-3-yl)pyrimidines

2021

Human African trypanosomiasis, or sleeping sickness, is a neglected tropical disease caused by Trypanosoma brucei rhodesiense and Trypanosoma brucei gambiense which seriously affects human health in Africa. Current therapies present limitations in their application, parasite resistance, or require further clinical investigation for wider use. Our work herein describes the design and syntheses of novel antitrypanosomal 4-phenyl-6-(pyridin-3-yl)pyrimidines, with compound 13, the 4-(2-methoxyphenyl)-6-(pyridine-3-yl)pyrimidin-2-amine demonstrating an IC50 value of 0.38 μM and a promising off-target ADME-Tox profile in vitro. In silico molecular target investigations showed rhodesain to be a pu…

Models MolecularTrypanosoma brucei rhodesiensepyrimidinessleeping sicknessIn silicoHuman african trypanosomiasis01 natural sciencesDockingCell Line03 medical and health sciencesantitrypanosomalDrug DiscoverymedicineAnimalsHumansAfrican trypanosomiasisIC50030304 developmental biologyrhodesainPharmacology0303 health sciences010405 organic chemistryChemistryDrug discoveryOrganic ChemistryAntitrypanosomalSleeping sicknessTrypanosoma brucei rhodesienseGeneral MedicineHuman African Trypanosomiasismedicine.diseaseTrypanocidal AgentsIn vitroRats0104 chemical sciencesPyrimidinesRhodesainTrypanosomiasis AfricanBiochemistryDrug developmentDocking (molecular)dockingADME-ToxResearch Paper
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In vitro and in silico studies of polycondensed diazine systems as anti-parasitic agents

2012

Abstract Parasitic diseases caused by protozoarian agents are still relevant today more than ever. Recently, we synthesized several polycondensed diazine derivatives by means 1,3-dipolar cycloaddition reactions. A broad selection of these compounds were submitted to in vitro biological screening against Plasmodium falciparum , Leishmania infantum , Trypanosoma brucei , and Trypanosoma cruzi , resulting active at micromolar level. Induced Fit Docking/MM-GBSA studies were performed giving interesting indications about the probable mechanism of action of the most active compounds

Models MolecularTrypanosoma cruziIn silicoPlasmodium falciparumTrypanosoma brucei bruceiClinical BiochemistryPharmaceutical ScienceTrypanosoma bruceiBiochemistryStructure-Activity Relationshipchemistry.chemical_compoundParasitic Sensitivity Testsparasitic diseasesDrug DiscoveryLeishmania infantumTrypanosoma cruziMolecular BiologyDiazineAntiparasitic AgentsDose-Response Relationship DrugMolecular StructurebiologyOrganic ChemistryPlasmodium falciparumAnti-parasitic Plasmodium Leishmania Trypanosoma Diazine Induced fit docking/MM-GBSAbiology.organism_classificationSettore CHIM/08 - Chimica FarmaceuticaHydrazineschemistryBiochemistryDocking (molecular)TrypanosomaMolecular MedicineLeishmania infantumBioorganic & Medicinal Chemistry Letters
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The Structure of Rauvolfia serpentina Strictosidine Synthase Is a Novel Six-Bladed β-Propeller Fold in Plant Proteins

2006

Abstract The enzyme strictosidine synthase (STR1) from the Indian medicinal plant Rauvolfia serpentina is of primary importance for the biosynthetic pathway of the indole alkaloid ajmaline. Moreover, STR1 initiates all biosynthetic pathways leading to the entire monoterpenoid indole alkaloid family representing an enormous structural variety of ∼2000 compounds in higher plants. The crystal structures of STR1 in complex with its natural substrates tryptamine and secologanin provide structural understanding of the observed substrate preference and identify residues lining the active site surface that contact the substrates. STR1 catalyzes a Pictet-Spengler–type reaction and represents a novel…

Models MolecularTryptamineProtein FoldingStrictosidine synthaseProtein ConformationMolecular Sequence DataSequence alignmentPlant ScienceCatalysisRauwolfiaSubstrate Specificitychemistry.chemical_compoundRauvolfia serpentinaCarbon-Nitrogen LyasesAmino Acid SequenceResearch ArticlesConserved SequencePlant ProteinsBinding SitesSequence Homology Amino AcidbiologyIndole alkaloidActive siteCell BiologyLyasebiology.organism_classificationTryptamineschemistryBiochemistrybiology.proteinSecologaninSequence AlignmentThe Plant Cell
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8-N(3)-3'-biotinyl-ATP, a novel monofunctional reagent: differences in the F(1)- and V(1)-ATPases by means of the ATP analogue.

2001

A novel photoaffinity label, 8-N(3)-3'-biotinyl-ATP, has been synthesized. The introduction of an additional biotin residue is advantageous for easy detection of labeled proteins. This could be first tested by reaction with the F(1)-ATPase from the thermophilic bacterium PS3 (TF(1)). UV irradiation of TF(1) in the presence of 8-N(3)-3'-biotinyl-ATP results in a nucleotide-dependent binding of the analogue in the noncatalytic alpha and the catalytic beta subunits of TF(1), demonstrating the suitability of this analogue as a potential photoaffinity label. Reaction with the V(1)-ATPase, however, led to labeling of subunit E, which has been suggested as a structural and functional homologue of …

Models MolecularVacuolar Proton-Translocating ATPasesTime FactorsUltraviolet RaysProtein subunitATPaseBiophysicsCoated vesicleBiotinPhotoaffinity LabelsPhotoaffinity LabelsBiochemistryCatalysischemistry.chemical_compoundAdenosine TriphosphateBiotinBacterial ProteinsManducaAnimalsBinding siteMolecular BiologyBinding SitesPhotoaffinity labelingbiologyChemistryCell BiologyProton-Translocating ATPasesBiochemistryModels ChemicalSpectrophotometrySpectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinCattleGamma subunitProtein BindingBiochemical and biophysical research communications
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Structural and magnetic investigations of the mixed-valence Fe(II,III) two-dimensional layer complex, [Fe2(II) Fe2(III)(HCOO)10(C6H7N)6]n.

2004

The structure of the complex, [Fe2(II)Fe2(III)(HCOO)10(C6H7N6)n, (1) exhibits a neutral two-dimensional layer network of alternating iron(II) and iron(III) ions, bridged equatorially by formate groups. All iron atoms are octahedrally coordinated, with iron(III) coordinating axially to one gamma-picoline and one formate group, while the iron(II) centers interact axially with two gamma-picoline groups, above and below the layer plane. The complex crystallizes in the triclinic space group P1 at all studied temperatures [at 120 K, the cell dimensions are: a = 10.228(1), b = 12.071(1), c = 12.072(1) A, alpha = 89.801(2), beta = 71.149(2), gamma = 73.371(2) degrees]. An intralayer antiferromagnet…

Models MolecularValence (chemistry)ChemistryStereochemistryExchange interactionTemperatureCrystal structureTriclinic crystal systemCrystallography X-RayMagnetic susceptibilityFerric CompoundsAtomic and Molecular Physics and OpticsCrystallographyMagneticsSpectroscopy MossbauerMössbauer spectroscopyOrganometallic CompoundsAntiferromagnetismMoleculeFerrous CompoundsPhysical and Theoretical ChemistryChemphyschem : a European journal of chemical physics and physical chemistry
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A novel caryophyllene type sesquiterpene lactone from Asparagus falcatus (Linn.); Structure elucidation and anti-angiogenic activity on HUVECs

2011

Abstract In this study the novel caryophyllene type sesquiterpene lactone (aspfalcolide) has been isolated from the leaves of Asparagus falcatus (Linn.) and characterized by IR, 1D NMR, 2D NMR, EI–MS, HR–ESI–MS and X-ray single crystal diffraction analysis. The aspfalcolide crystallizes in the orthorhombic space group P212121 with a = 6.37360(10), b = 7.6890(2), c = 27.3281(6) A, α = β = γ = 90° and Z = 4. One intermolecular O–H⋯O hydrogen bond enforces these natural molecules to form infinite chains through the crystal. Aspfalcolide was screened for its anti-angiogenic activity in human umbilical vein endothelial cells (HUVECs) and the result showed the remarkable inhibitory effect of aspf…

Models MolecularVascular Endothelial Growth Factor AStereochemistryMolecular ConformationAngiogenesis InhibitorsSesquiterpene lactoneUmbilical veinLactoneschemistry.chemical_compoundCell MovementDrug DiscoveryHuman Umbilical Vein Endothelial CellsHumansta116Cell ProliferationAsparagus falcatusPolycyclic SesquiterpenesPharmacologychemistry.chemical_classificationTube formationbiologyHydrogen bondCaryophylleneOrganic ChemistryGeneral Medicinebiology.organism_classificationchemistryOrthorhombic crystal systemAsparagus PlantSesquiterpenesTwo-dimensional nuclear magnetic resonance spectroscopyEuropean Journal of Medicinal Chemistry
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Identification of SNARE complex modulators that inhibit exocytosis from an alpha-helix-constrained combinatorial library.

2003

Synthetic peptides patterned after the proteins involved in vesicle fusion [the so-called SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) proteins] are potent inhibitors of SNARE complex assembly and neuronal exocytosis. It is noteworthy that the identification of peptide sequences not related to the SNARE proteins has not been accomplished yet; this is due, in part, to the structural constraints and the specificity of the protein interactions that govern the formation of the SNARE complex. Here we have addressed this question and used a combinatorial approach to identify peptides that modulate the assembly of the SNARE core complex and inhibit neuronal…

Models MolecularVesicle fusionMacromolecular SubstancesChromaffin CellsMolecular Sequence DataVesicular Transport ProteinsBiologyBiochemistryExocytosisExocytosisProtein Structure SecondaryPeptide LibraryAnimalsAmino Acid SequencePeptide libraryMolecular BiologyCells CulturedSNARE complex assemblyNeuronsSTX1AMembrane ProteinsMunc-18Cell BiologyFusion proteinCell biologyRatsCattleSNARE complexPeptidesSNARE ProteinsResearch ArticleThe Biochemical journal
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Molecular and topological membrane folding determinants of transient receptor potential vanilloid 2 channel.

2015

Transient Receptor Potential (TRP) channels are related to adaptation to the environment and somatosensation. The transient receptor potential vanilloid (TRPV) subfamily includes six closely evolutionary related ion channels sharing the same domain organization and tetrameric arrangement in the membrane. In this study we have characterized biochemically TRPV2 channel membrane protein folding and transmembrane (TM) architecture. Deleting the first N-terminal 74 residues preceding the ankyrin repeat domain (ARD) show a key role for this region in targeting the protein to the membrane. We have demonstrated the co-translational insertion of the membrane-embedded region of the TRPV2 and its disp…

Models MolecularVesicle-associated membrane protein 8Protein FoldingTRPV5Protein ConformationBiophysicsTRPV Cation ChannelsBiochemistryTRPVTransient receptor potential channelAnimalsHumansProtein Structure QuaternaryMolecular BiologyIon channelTransmembrane channelsChemistryCell MembraneCell BiologyTransmembrane proteinRecombinant ProteinsAnkyrin RepeatProtein Structure TertiaryRatsHEK293 CellsBiochemistryBiophysicsAnkyrin repeatBiochemical and biophysical research communications
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Oligomerization of polytopic α-helical membrane proteins: causes and consequences

2012

Abstract Several polytopic α-helical membrane-integrated proteins appear to be organized in higher-ordered oligomeric complexes. While many aspects are still enigmatic, in recent years, the physiological impact of membrane protein oligomerization has been analyzed to some extent. In the present article, oligomerization of structurally well-defined membrane proteins is discussed. The available experimental information indicates the causes and physiological consequences of membrane protein oligomerization, including stabilization, cooperative functions, and control of specific activities. Based on the currently available observations, we aim to derive some general principles and discuss open …

Models MolecularVesicle-associated membrane protein 8Protein StabilityChemistryClinical BiochemistryPeripheral membrane proteinMembrane ProteinsBiochemistryProtein Structure SecondaryMembrane proteinBiochemistryα helicalBiophysicsHumansMolecular BiologyIntegral membrane proteinFunction (biology)G protein-coupled receptorbchm
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A molecular assembly system that renders antigens of choice highly repetitive for induction of protective B cell responses.

2002

Virus like particles (VLPs) are known to induce potent B cell responses in the absence of adjuvants. Moreover, epitope-specific antibody responses may be induced by VLPs that contain peptides inserted in their immunodominant regions. However, due to steric problems, the size of the peptides capable of being incorporated into VLPs while still permitting capsid assembly, is rather limited. While peptides genetically fused to either the N- or C-terminus of VLPs present fewer assembly problems, the immune responses obtained against such epitopes are often limited, most likely because the epitopes are not optimally exposed. In addition, such particles may be less stable in vivo. Here, we show th…

Models MolecularViral Hepatitis VaccinesHepatitis B virusMacromolecular SubstancesProtein ConformationvirusesRecombinant Fusion ProteinsProtozoan ProteinsAntigens ProtozoanBiologyProtein EngineeringEpitopePhospholipases AInclusion Bodies ViralViral Matrix ProteinsMiceImmune systemAntigenVirus-like particlemedicineAnimalsB cellB-LymphocytesMice Inbred BALB CVaccines SyntheticGeneral VeterinaryGeneral Immunology and MicrobiologyImmunodominant EpitopesImmunogenicityVaccinationPublic Health Environmental and Occupational HealthMolecular biologyHepatitis B Core AntigensPeptide FragmentsCell biologyProtein Structure TertiaryHBcAgBee VenomsInfectious Diseasesmedicine.anatomical_structureCross-Linking ReagentsCapsidDrug DesignMolecular MedicineFemaleImmunizationPeptidesOligopeptidesVaccine
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