Search results for "binding site"

showing 10 items of 856 documents

Bioorganic/inorganic hybrid composition of sponge spicules: matrix of the giant spicules and of the comitalia of the deep sea hexactinellid Monorhaph…

2007

The giant basal spicules of the siliceous sponges Monorhaphis chuni and Monorhaphis intermedia (Hexactinellida) represent the largest biosilica structures on earth (up to 3 m long). Here we describe the construction (lamellar organization) of these spicules and of the comitalia and highlight their organic matrix in order to understand their mechanical properties. The spicules display three distinct regions built of biosilica: (i) the outer lamellar zone (radius: >300 mu m), (ii) the bulky axial cylinder (radius: <75 mu m), and (iii) the central axial canal (diameter: <2 mu m) with its organic axial filament. The spicules are loosely covered with a collagen net which is regularly perforated …

SpiculeMaterials scienceBinding SitesbiologyHexactinellidScanning electron microscopebiology.organism_classificationPoriferaCrystallographySponge spiculeStructural BiologyMicroscopy Electron ScanningAnimalsLamellar structureCollagenComposite materialElasticity (economics)PorosityDissolutionPeptide HydrolasesJournal of structural biology
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Identification of a silicatein(-related) protease in the giant spicules of the deep-sea hexactinellid Monorhaphis chuni.

2008

SUMMARYSilicateins, members of the cathepsin L family, are enzymes that have been shown to be involved in the biosynthesis/condensation of biosilica in spicules from Demospongiae (phylum Porifera), e.g. Tethya aurantium and Suberites domuncula. The class Hexactinellida also forms spicules from this inorganic material. This class of sponges includes species that form the largest biogenic silica structures on earth. The giant basal spicules from the hexactinellids Monorhaphis chuni and Monorhaphis intermedia can reach lengths of up to 3 m and diameters of 10 mm. The giant spicules as well as the tauactines consist of a biosilica shell that surrounds the axial canal, which harbours the axial f…

SpiculePhysiologyOceans and SeasMolecular Sequence DataAquatic ScienceCysteine Proteinase InhibitorsCathepsin LDemospongeSponge spiculeAnimalsAmino Acid SequenceTethya aurantiumMolecular BiologyEcology Evolution Behavior and SystematicsPhylogenyBinding SitesbiologyHexactinellidAnimal StructuresAnatomybiology.organism_classificationCathepsinsCystatinsPoriferaSuberites domunculaMolecular WeightSpongeBiochemistryInsect ScienceMolecular Probesbiology.proteinAnimal Science and ZoologyProtein Processing Post-TranslationalThe Journal of experimental biology
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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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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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Design and synthesis of pironetin analogue/colchicine hybrids and study of their cytotoxic activity and mechanisms of interaction with tubulin

2014

We here report the synthesis of a series of 12 hybrid molecules composed of a colchicine moiety and a pironetin analogue fragment. The two fragments are connected through an ester-amide spacer of variable length. The cytotoxic activities of these compounds and their interactions with tubulin have been investigated. Relations between the structure and activity are discussed. Since the spacer is not long enough to permit a simultaneous binding of the hybrid molecules to the colchicine and pironetin sites on tubulin, a further feature investigated was whether these molecules would interact with the latter through the pironetin end (irreversible covalent binding) or through the colchicine end (…

StereochemistryChemical structureCellsFluorescent Antibody TechniqueAntineoplastic AgentsLigandsMicrotubulespironetinStructure-Activity Relationshipchemistry.chemical_compoundChemical structureTubulinNeoplasmsDrug DiscoveryTumor Cells CulturedHumansColchicineMoietyMoleculeStructure–activity relationshipBinding siteCell ProliferationPharmacologyBinding SitesDrug effectsMolecular StructurebiologyToxicityCell growthMoleculesTubulinchemistryPyronesDrug Designbiology.proteinMolecular MedicineColchicineJournal of Medicinal Chemistry
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