Search results for "binding site"

showing 10 items of 856 documents

Kinetic properties of hexameric tyrosinase from the crustacean Palinurus elephas.

2008

Tyrosinases catalyze hydroxylation of monophenols to o-diphenols and their subsequent oxidation to o-quinones, whereas catecholoxidases catalyze only the latter reaction. Both enzymes occur in all organisms and are Type 3 copper proteins that perform the first steps of melanin formation. In arthropods, they play an essential role in the sclerotization of the exoskeleton. Very few phenoloxidases are characterized structurally or kinetically and the existence of an actual tyrosinase activity has not been demonstrated in most cases. Here we present for the first time a complete kinetic characterization of a tyrosinase from a crustacean (Palinurus elephas) including the influence of inhibitors.…

StereochemistryCopper proteinTyrosinaseDopamineAllosteric regulationTyramineCooperativityBiologyBiochemistryBinding CompetitiveHydroxylationchemistry.chemical_compoundNon-competitive inhibitionAnimalsMimosinePhysical and Theoretical ChemistryEnzyme InhibitorsPalinuridaechemistry.chemical_classificationBinding SitesMolecular StructureMonophenol MonooxygenaseGeneral MedicinePhenylthioureaKineticsEnzymechemistryBiochemistryMimosineAllosteric SitePhotochemistry and photobiology
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Molecular topology applied to the discovery of 1-benzyl-2-(3-fluorophenyl)-4-hydroxy-3-(3-phenylpropanoyl)-2H-pyrrole-5-one as a non-ligand-binding-p…

2014

We report the discovery of 1-benzyl-2-(3- fluorophenyl)-4-hydroxy-3-(3-phenylpropanoyl)-2H-pyrrole- 5-one as a novel non-ligand binding pocket (non-LBP) antagonist of the androgen receptor (AR) through the application of molecular topology techniques. This compound, validated through time-resolved fluorescence resonance energy transfer and fluorescence polarization biological assays, provides the basis for lead optimization and structure−activity relationship analysis of a new series of non-LBP AR antagonists. Induced-fit docking and molecular dynamics studies have been performed to establish a consistent hypothesis for the interaction of the new active molecule on the AR surface. Refereed/…

StereochemistryGeneral Chemical EngineeringMolecular ConformationLibrary and Information SciencesMolecular Dynamics Simulationmolecular topologySmall Molecule LibrariesMolecular dynamicschemistry.chemical_compoundStructure-Activity RelationshipUser-Computer Interfaceexperimental validationDrug DiscoveryFluorescence Resonance Energy TransferMoleculeHumansPyrrolesPyrroleBinding SitesChemistryAntagonistAndrogen AntagonistsGeneral Chemistryvirtual screeningComputer Science ApplicationsHigh-Throughput Screening AssaysAndrogen receptorMolecular Docking SimulationFörster resonance energy transferDocking (molecular)Receptors AndrogenThermodynamicsFluorescence anisotropyProtein Binding
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Synthesis and Characterization of New Bivalent Agents as Melatonin- and Histamine H3-Ligands

2014

Melatonin is an endogenous molecule involved in many pathophysiological processes. In addition to the control of circadian rhythms, its antioxidant and neuroprotective properties have been widely described. Thus far, different bivalent compounds composed by a melatonin molecule linked to another neuroprotective agent were synthesized and tested for their ability to block neurodegenerative processes in vitro and in vivo. To identify a novel class of potential neuroprotective compounds, we prepared a series of bivalent ligands, in which a prototypic melatonergic ligand is connected to an imidazole-based H3 receptor antagonist through a flexible linker. Four imidazolyl-alkyloxy-anilinoethylami…

StereochemistryHistamine AntagonistsLigandsMelatonin receptorMT<sub>2</sub>ArticleCatalysisInorganic Chemistrylcsh:ChemistryHistamine receptorPiperidinesH<sub>3</sub> antagonistsHumansReceptors Histamine H3Physical and Theoretical ChemistryBinding siteReceptormelatonin receptorMolecular Biologylcsh:QH301-705.5SpectroscopyBinding SitesReceptor Melatonin MT2ChemistryReceptor Melatonin MT1MT1Organic ChemistryMT2ImidazolesHistaminergicMT<sub>1</sub>General Medicinemelatonin receptor; MT1; MT2; H3 antagonists; bivalent ligandsLigand (biochemistry)Protein Structure TertiaryComputer Science ApplicationsMelatonergicMolecular Docking SimulationBiochemistrylcsh:Biology (General)lcsh:QD1-999bivalent ligandsHistamine H3 receptorH3 antagonistsProtein BindingInternational Journal of Molecular Sciences
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α-Adrenoceptor Interaction of Tetrandrine and Isotetrandrine in the Rat: Functional and Binding Assays

1998

Abstract The action of 1S,1′S-tetrandrine, a bisbenzyltetrahydroisoquinoline alkaloid, on α1-adrenoceptors has been compared with that of its isomer 1R,1′S-isotetrandrine. The work includes binding assays to analyse the affinity of these products for the [3H]prazosin binding site of rat cerebral cortical membranes and functional studies on rat isolated aorta to examine the effects of both alkaloids on intracellular calcium processes related or not to α-adrenoceptor activation. A radioligand receptor-binding study showed that both compounds interacted with the α1-adrenoceptors displacing [3H]prazosin from the specific binding site. The Ki values (inhibition constants) were 0.69±0.12 and 1.6±…

StereochemistryPharmaceutical Sciencechemistry.chemical_elementAorta ThoracicIn Vitro TechniquesBiologyPharmacologyCalciumTritiumBenzylisoquinolinesBinding CompetitiveMuscle Smooth VascularCalcium in biologyNorepinephrinechemistry.chemical_compoundAlkaloidsPrazosinmedicineExtracellularAnimalsDrug InteractionsRats WistarCerebral CortexPharmacologyBinding SitesMolecular StructureAlkaloidBiological activityPrazosinReceptors Adrenergic alphaCalcium Channel BlockersRatsTetrandrinechemistryCalciumFemaleIntracellularMuscle ContractionProtein Bindingmedicine.drugJournal of Pharmacy and Pharmacology
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A second pathway of activation of the Torpedo acetylcholine receptor channel

1991

We have studied the interaction of the reversible acetylcholine esterase inhibitor (-)physostigmine (D-eserine) with the nicotinic acetylcholine receptor (nAChR) from Torpedo marmorata electric tissue by means of ligand-induced ion flux into nAChR-rich membrane vesicles and of equilibrium binding. We find that (-) physostigmine induces cation flux (and also binds to the receptor) even in the presence of saturating concentrations of antagonists of acetylcholine, such as D-tubocurarine, alpha-bungarotoxin or antibody WF6. The direct action on the acetylcholine receptor is not affected by removal of the methylcarbamate function from the drug and thus is not due to carbamylation of the receptor…

StereochemistryPhysostigmineCesiumTubocurarineReceptors NicotinicTorpedoBiochemistryIon ChannelsAcetylcholine bindingCationsMuscarinic acetylcholine receptor M5medicineAnimalsBinding siteAcetylcholine receptorElectric OrganBinding SitesChemistryCell MembraneAntibodies MonoclonalMuscarinic acetylcholine receptor M3BungarotoxinsQuaternary Ammonium CompoundsNicotinic acetylcholine receptorNicotinic agonistBiophysicsCarbamatesAcetylcholinemedicine.drugEuropean Journal of Biochemistry
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Attracted or repelled?--a matter of two neurons, one pheromone binding protein, and a chiral center.

1998

Abstract Two species of scarab beetles, the Osaka beetle (Anomala osakana) and the Japanese beetle (Popillia japonica), utilize the opposite enantiomers of japonilure, (Z)-5-(1-decenyl)oxacyclopentan-2-one, as their sex pheromones. Each species produces only one of the enantiomers that functions as its own sex pheromone and as a very strong behavioral antagonist for the other species. Using an integrated approach we tested whether the discrimination of these two opposite signals is due to selective filtering by pheromone binding proteins or whether it originates in the specificity of ligand–receptor interactions. We found that the antennae of each of these two scarab species contain only a …

StereochemistryProtein ConformationMolecular Sequence DataBiophysicsBiochemistryPheromonesPopilliaBotanymedicineAnimalsPheromone bindingAmino Acid SequenceCloning MolecularMolecular BiologySensillumNeuronsOlfactory receptorBinding SitesbiologyStereoisomerismCell Biologybiology.organism_classificationChemoreceptor CellsColeopteramedicine.anatomical_structureSex pheromonePheromoneEnantiomerPheromone binding proteinSequence AlignmentSignal TransductionBiochemical and biophysical research communications
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Efficient synthesis of hexahydroindenopyridines and their potential as melatoninergic ligands.

2014

Hexahydroindenopyridine (HHIP) is an interesting tricyclic piperidine nucleus that is structurally related to melatonin, a serotonin-derived neurohormone. Melatonin receptor ligands have applications in several cellular, neuroendocrine and neurophysiological disorders, including depression and/or insomnia. We report herein an efficient two-step method to prepare new HHIP via enamine C-alkylation-cyclization. The influence of substituents on the benzene ring and the nitrogen atom on melatoninergic receptors has been studied. Among the 25 synthesized HHIPs, some of them containing methylenedioxy (series 2) and 8-chloro-7-methoxy substituents (series 4) on the benzene ring revealed affinity fo…

StereochemistryPyridinesRing (chemistry)LigandsMelatonin receptorMethylenedioxyEnaminechemistry.chemical_compoundStructure-Activity RelationshipDrug DiscoveryHumansReceptorCells CulturedPharmacologychemistry.chemical_classificationBinding SitesDose-Response Relationship DrugMolecular StructureReceptor Melatonin MT2Receptor Melatonin MT1Organic ChemistryGeneral MedicineHEK293 CellschemistryPiperidineAcetamideTricyclicEuropean journal of medicinal chemistry
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The mechanism of hydrolysis of beta-glycerophosphate by kidney alkaline phosphatase.

1975

1. To identify the functional groups that are involved in the conversion of β-glycerophosphate by alkaline phosphatase (EC 3.1.3.1) from pig kidney, the kinetics of alkaline phosphatase were investigated in the pH range 6.6-10.3 at substrate concentrations of 3 μM-30 mM. From the plots of log ṼH+ against pH and log ṼH+/KH+m against pH one functional group with pK = 7.0 and two functional groups with pK = 9.1 were identified. These groups are involved in substrate binding. Another group with pK = 8.8 was found, which in its unprotonated form catalyses substrate conversion. 2. GSH inhibits the alkaline phosphatase reversibly and non-competitively by attacking the bound Zn(II). 3. The influenc…

StereochemistrySwineKidneyBiochemistrychemistry.chemical_compoundHydrolysisAnimalsMagnesiumBinding siteMolecular Biologychemistry.chemical_classificationBinding SitesHydrolysisSubstrate (chemistry)Cell BiologyGlutathioneHydrogen-Ion ConcentrationPhosphateAlkaline PhosphataseGlutathioneKineticsZincEnzymechemistryModels ChemicalGlycerophosphatesFunctional groupAlkaline phosphataseResearch ArticleThe Biochemical journal
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Multipolar interactions in the D pocket of thrombin: large differences between tricyclic imide and lactam inhibitors.

2006

Two series of tricyclic inhibitors of the serine protease thrombin, imides (+/-)-1-(+/-)-8 and lactams (+/-)-9-(+/-)-13, were analysed to evaluate contributions of orthogonal multipolar interactions with the backbone C=O moiety of Asn98 to the free enthalpy of protein-ligand complexation. The lactam derivatives are much more potent and more selective inhibitors (K(i) values between 0.065 and 0.005 microM, selectivity for thrombin over trypsin between 361- and 1609-fold) than the imide compounds (Ki values between 0.057 and 23.7 microM, selectivity for thrombin over trypsin between 3- and 67-fold). The increase in potency and selectivity is explained by the favorable occupancy of the P-pocke…

Steric effectsSerine Proteinase InhibitorsLactamsStereochemistrySubstituentCrystallography X-RayImidesBiochemistrychemistry.chemical_compoundThrombinmedicineMoietyPhysical and Theoretical ChemistryImideBinding SitesLigandOrganic ChemistryThrombinKineticschemistryModels ChemicalCyclizationLactamIsopropylmedicine.drugProtein BindingOrganicbiomolecular chemistry
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ChIP-Seq from Limited Starting Material of K562 Cells and Drosophila Neuroblasts Using Tagmentation Assisted Fragmentation Approach

2019

Chromatin immunoprecipitation is extensively used to investigate the epigenetic profile and transcription factor binding sites in the genome. However, when the starting material is limited, the conventional ChIP-Seq approach cannot be implemented. This protocol describes a method that can be used to generate the chromatin profiles from as low as 100 human or 1,000 Drosophila cells. The method employs tagmentation to fragment the chromatin with concomitant addition of sequencing adaptors. The method generates datasets with high signal to noise ratio and can be subjected to standard tools for ChIP-Seq analysis.

Strategy and ManagementMechanical EngineeringSystems biologyMetals and AlloysGenomicsComputational biologyGenomeIndustrial and Manufacturing EngineeringDNA sequencingChromatinDNA binding siteEpigenetic ProfileMethods ArticleChromatin immunoprecipitation
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