Search results for "binding"

showing 10 items of 3896 documents

NineTeen Complex-subunit Salsa is required for efficient splicing of a subset of introns and dorsal-ventral patterning

2020

© 2020 Rathore et al. This article is distributed exclusively by the RNASociety for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

SpliceosomeBiochemistry & Molecular BiologyRNA SplicingBiologySplicingGermlineArticleMidblastulaDorsal-ventral patterning03 medical and health sciencesAnimalsDrosophila ProteinsFemale fertilityGurkenMolecular BiologyGene030304 developmental biologyBody Patterning0303 health sciencesMessenger RNA030302 biochemistry & molecular biologyfungiIntronGene Expression Regulation DevelopmentalTransforming Growth Factor alphaRNA Helicase AIntronsCell biologyDorsal-ventral patterning; Drosophila; Female fertility; Gurken; Splicing; dorsal–ventral patterning; female fertility; splicingDNA-Binding ProteinsDrosophila melanogasterRNA splicingSpliceosomesFemaleDrosophilaInfertility Female
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Albumin-driven disassembly of lipidic nanoparticles: the specific case of the squalene-adenosine nanodrug

2020

International audience; In the field of nanomedicine, nanostructured nanoparticles (NPs) made of self-assembling prodrugs emerged in the recent years with promising properties. In particular, squalene-based drug nanoparticles have already shown their efficiency through in vivo experiments. However, a complete pattern of their stability and interactions in the blood stream is still lacking. In this work we assess the behavior of squalene-adenosine (SQAd) nanoparticles-whose neuroprotective effect has already been demonstrated in murine models-in the presence of fetal bovine serum (FBS) and of bovine serum albumin (BSA), the main protein of blood plasma. Extensive physicochemical characteriza…

SqualeneAdenosinecomplexationserum albuminSerum albumin02 engineering and technologyPlasma protein binding010402 general chemistry01 natural sciencesMiceDrug StabilitymedicineAnimalsHumansGeneral Materials ScienceProdrugsColloidsBovine serum albuminComputingMilieux_MISCELLANEOUSBinding Sitesbiology[CHIM.ORGA]Chemical Sciences/Organic chemistryChemistryAlbuminIsothermal titration calorimetry[CHIM.MATE]Chemical Sciences/Material chemistry021001 nanoscience & nanotechnologyHuman serum albumindisassembly0104 chemical sciencesnanodrugbiology.proteinBiophysicsNanomedicineNanoparticles0210 nano-technologyFetal bovine serummedicine.drugProtein Binding
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Low density lipoproteins and human serum albumin as the carriers of squalenoylated drugs: insights from molecular simulations

2018

We have studied the interaction of three clinically promising squalenoylated drugs (gemcitabine-squalene, adenine-squalene, and doxorubicin-squalene) with low-density lipoproteins (LDL) by means of atomistic molecular dynamics simulations. It is shown that all studied squalenoylated drugs accumulate inside the LDL particles. This effect is promoted by the squalene moiety, which acts as an anchor and drives the hydrophilic drugs into the hydrophobic core of the LDL lipid droplet. Our data suggest that LDL particles could be a universal carriers of squalenoylated drugs in the bloodstream. Interaction of gemcitabine-squalene with human serum albumin (HSA) was also studied by ensemble of dockin…

Squalene[PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph]Drug CompoundingPharmaceutical ScienceSerum Albumin Human02 engineering and technologyPlasma protein bindingMolecular Dynamics Simulation010402 general chemistry01 natural sciencesMolecular Docking SimulationDeoxycytidineSqualenechemistry.chemical_compound[ PHYS.PHYS.PHYS-BIO-PH ] Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph]Lipid dropletDrug DiscoverymedicineMoietyHumansComputingMilieux_MISCELLANEOUSDrug CarriersBinding SitesAdenine[SDV.SP]Life Sciences [q-bio]/Pharmaceutical sciences021001 nanoscience & nanotechnologyHuman serum albuminGemcitabine3. Good health0104 chemical sciences[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryLipoproteins LDLMolecular Docking Simulation[ SDV.SP ] Life Sciences [q-bio]/Pharmaceutical scienceschemistryDocking (molecular)Doxorubicin[ CHIM.THEO ] Chemical Sciences/Theoretical and/or physical chemistryBiophysicsMolecular MedicineNanoparticles0210 nano-technologyDrug carrierHydrophobic and Hydrophilic Interactionsmedicine.drugProtein Binding
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Lipid and phase specificity of α-toxin from S. aureus

2013

AbstractThe pore forming toxin Hla (α-toxin) from Staphylococcus aureus is an important pathogenic factor of the bacterium S. aureus and also a model system for the process of membrane-induced protein oligomerisation and pore formation. It has been shown that binding to lipid membranes at neutral or basic pH requires the presence of a phosphocholine-headgroup. Thus, sphingomyelin and phosphatidylcholine may serve as interaction partners in cellular membranes. Based on earlier studies it has been suggested that rafts of sphingomyelin are particularly efficient in toxin binding. In this study we compared the oligomerisation of Hla on liposomes of various lipid compositions in order to identif…

Staphylococcus aureusPore formationLiquid ordered phaseBacterial ToxinsLipid BilayersBiophysicsBiologyBiochemistryPhase Transitionchemistry.chemical_compoundHemolysin ProteinsMembrane LipidsMembrane MicrodomainsPhosphatidylcholineBinding siteLipid raftUnilamellar LiposomesPore-forming toxinLiposomeArtificial membranesBinding SitesCell MembraneOligomerisationCell BiologyS. aureusSphingomyelinsMembraneBiochemistrychemistryMicroscopy FluorescenceMutationPhosphatidylcholineslipids (amino acids peptides and proteins)Protein MultimerizationToxinSphingomyelinBiochimica et Biophysica Acta (BBA) - Biomembranes
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The hemagglutinin of Staphylococcus saprophyticus is a major adhesin for uroepithelial cells.

1996

The 160-kDa hemagglutinin of Staphylococcus saprophyticus also serves as a fibronectin-binding protein, and the two activities may be present on different parts of the molecule. Bacteria expressing the 160-kDa hemagglutinin bound in large numbers to histological sections of human ureters, whereas nonhemagglutinating bacteria did not bind. Binding was decreased by an antiserum to the 160-kDa protein and by a preparation of sheep erythrocyte membranes. Fibronectin had no effect. We therefore conclude that binding of S. saprophyticus to uroepithelial cells is mediated by the hemagglutinating activity of the 160-kDa surface protein.

StaphylococcusImmunologyBiologymedicine.disease_causeMicrobiologyBacterial AdhesionEpitheliumMicrobiologymedicineAnimalsHumansAntiserumchemistry.chemical_classificationStaphylococcus saprophyticusSheepBinding proteinErythrocyte MembraneHemagglutininbiology.organism_classificationFibronectinsBacterial adhesinInfectious DiseasesHemagglutininschemistryParasitologyUreterGlycoproteinStaphylococcusBacteriaResearch ArticleInfection and immunity
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Synthesis and biological evaluation of 2- and 3-aminobenzo[b]thiophene derivatives as antimitotic agents and inhibitors of tubulin polymerization.

2007

Two new series of inhibitors of tubulin polymerization based on the 2-amino-3-(3,4,5-trimethoxybenzoyl)benzo[b]thiophene molecular skeleton and its 3-amino positional isomer were synthesized and evaluated for antiproliferative activity, inhibition of tubulin polymerization, and cell cycle effects. Although many more 3-amino derivatives have been synthesized so far, the most promising compound in this series was 2-amino-6-methyl-3-(3,4,5-trimethoxybenzoyl)benzo[b]thiophene, which inhibits cancer cell growth at subnanomolar concentrations and interacts strongly with tubulin by binding to the colchicine site.

StereochemistryAntimitotic Agents/chemistry Antimitotic Agents/pharmacologymacromolecular substancesThiophenesAntimitotic AgentsChemical synthesischemistry.chemical_compoundMiceRadioligand AssayStructure-Activity RelationshipTubulinCell Line TumorDrug DiscoveryThiopheneStructure–activity relationshipAnimalsHumansCytotoxicityCell ProliferationBinding SitesbiologyBicyclic moleculeChemistryTubulin ModulatorsCell CycleTubulin ModulatorsTubulinbiology.proteinMolecular MedicineAntimitotic AgentDrug Screening Assays AntitumorColchicineProtein BindingJournal of medicinal chemistry
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Binding isotope effects as a tool for distinguishing hydrophobic and hydrophilic binding sites of HIV-1 RT.

2014

The current treatment for HIV-1 infected patients consists of a cocktail of inhibitors, in an attempt to improve the potency of the drugs by adding the possible effects of each supplied compound. In this contribution, nine different inhibitors of HIV-1 RT, one of the three key proteins responsible for the virus replication, have been selected to develop and test a computational protocol that allows getting a deep insight into the inhibitors’ binding mechanism. The interaction between the inhibitors and the protein have been quantified by computing binding free energies through FEP calculations, while a more detailed characterization of the kind of inhibitor–protein interactions is based on …

StereochemistryBinding energyHuman immunodeficiency virus (HIV)Binding energyMolecular Dynamics Simulationmedicine.disease_causeLigandsIsotopesCatalytic DomainKinetic isotope effectDrug DiscoveryMaterials ChemistrymedicinePhysical and Theoretical ChemistryBinding siteBinding isotope effectsIsotopeChemistryWaterHIV Reverse TranscriptaseSurfaces Coatings and FilmsCrystallographyViral replicationHIV-1SolventsQuantum TheoryReverse Transcriptase InhibitorsThermodynamicsFree energiesHydrophobic and Hydrophilic InteractionsProtein BindingThe journal of physical chemistry. B
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Characterization of the binding of benzodiazepines to human serum albumin

1973

The binding of eleven benzodiazepine derivatives to human serum albumin (HSA) was determined by means of sephadex gel filtration. The albumin binding of the substances was characterized by the percentage of bound drug, the binding constants k +, K 1 and m, the number of binding sites per albumin molecule, and the free binding energy. Under the conditions chosen in these experiments there seems to exist only one binding site of the same type for all investigated benzodiazepines at the HSA molecule. The affinities of the benzodiazepines to this binding site are very different. It is discussed which part of the benzodiazepine molecule represents the main binding group.

StereochemistryBinding energySerum albuminPlasma protein bindingFlurazepammedicineHumansNitrazepamBovine serum albuminBinding siteSerum AlbuminPharmacologyBinding SitesbiologyOxazepamChemistryAlbuminChlordiazepoxideGeneral MedicineBenzazepinesHuman serum albuminSephadexChromatography Gelbiology.proteinProtein Bindingmedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
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Cherimolin-1, New Selective Inhibitor of the First Energy-Coupling Site of the NADH:Ubiquinone Oxidoreductase (Complex I)

1997

The mechanism linking electron transport to proton translocation in the NADH:ubiquinone oxidoreductase (complex I of the mitochondrial respiratory chain) is still unclear. Inhibitors acting at different sites of the enzyme are powerful tools to clarify this mechanism. Up to now, a unique inhibitor, the Annonaceous acetogenin rolliniastatin-2, selectively blocks the most internal proton-translocation site. This study introduces cherimolin-1, a new acetogenin that inhibits the complex I with this special mode of action, which is more easily available from the plant material. Moreover, the mode of action of this scarce type of complex I inhibitor is further characterized.

StereochemistryBiophysicsEnergy couplingBiologyBiochemistryLactonesStructure-Activity Relationshipchemistry.chemical_compoundOxidoreductaseNAD(P)H Dehydrogenase (Quinone)AnimalsStructure–activity relationshipFuransMode of actionMolecular Biologychemistry.chemical_classificationBinding SitesPlant ExtractsCell BiologyElectron transport chainEnzymeMitochondrial respiratory chainchemistryFruitAcetogeninCattleEnergy MetabolismBiochemical and Biophysical Research Communications
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Efficient synthesis and 5-LOX/COX-inhibitory activity of some 3-hydroxybenzo[b]thiophene-2-carboxylic acid derivatives

2012

Abstract A series of 3-hydroxybenzo[ b ]thiophene-2-carboxylic acid derivatives has been prepared and subsequently evaluated with regards to the inhibition of 5-LOX/COX. Structure optimization furnished derivatives with promising in vitro activity as dual 5-LOX/COX inhibitors with submicromolar IC 50 values for inhibition of 5-LOX and COX-1, respectively.

StereochemistryCarboxylic acidClinical BiochemistryCarboxylic AcidsPharmaceutical ScienceThiophenesInhibitory postsynaptic potentialBiochemistryStructure-Activity Relationshipchemistry.chemical_compoundDrug DiscoveryThiopheneCyclooxygenase InhibitorsLipoxygenase InhibitorsMolecular Biologychemistry.chemical_classificationArachidonate 5-Lipoxygenaseintegumentary systemOrganic Chemistryfood and beveragesBenzothiopheneIn vitrochemistryCyclooxygenase 1Molecular MedicineLicofeloneProtein BindingBioorganic & Medicinal Chemistry Letters
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