Search results for "allosteric site"

showing 10 items of 12 documents

Anti-inflammatory lipoxin A4 is an endogenous allosteric enhancer of CB1 cannabinoid receptor.

2012

Allosteric modulation of G-protein–coupled receptors represents a key goal of current pharmacology. In particular, endogenous allosteric modulators might represent important targets of interventions aimed at maximizing therapeutic efficacy and reducing side effects of drugs. Here we show that the anti-inflammatory lipid lipoxin A 4 is an endogenous allosteric enhancer of the CB 1 cannabinoid receptor. Lipoxin A 4 was detected in brain tissues, did not compete for the orthosteric binding site of the CB 1 receptor (vs. 3 H-SR141716A), and did not alter endocannabinoid metabolism (as opposed to URB597 and MAFP), but it enhanced affinity of anandamide at the CB1 receptor, thereby potentiating …

Cannabinoid receptorAllosteric regulationAnti-Inflammatory AgentsSpatial BehaviorEndogenyAmyloidogenic ProteinsMice TransgenicBiologyPharmacologyReceptors G-Protein-Coupled03 medical and health scienceschemistry.chemical_compoundMice0302 clinical medicineReceptor Cannabinoid CB1In vivoMemoryCommentariesAnimalsReceptor030304 developmental biologyInflammationMice Knockout0303 health sciencesMultidisciplinarymusculoskeletal neural and ocular physiologyBrainAnandamideURB597Biological SciencesEndocannabinoid system3. Good healthLipoxinsMice Inbred C57BLKineticsNeuroprotective Agentschemistrynervous systemlipids (amino acids peptides and proteins)030217 neurology & neurosurgerypsychological phenomena and processesAllosteric SiteEndocannabinoidsProceedings of the National Academy of Sciences of the United States of America
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Dynamic-shared Pharmacophore Approach as Tool to Design New Allosteric PRC2 Inhibitors, Targeting EED Binding Pocket.

2020

Abstract: The Polycomb Repressive complex 2 (PRC2) maintains a repressive chromatin state and silences many genes, acting as methylase on histone tails. This enzyme was found overexpressed in many types of cancer. In this work, we have set up a Computer-Aided Drug Design approach based on the allosteric modulation of PRC2. In order to minimize the possible bias derived from using a single set of coordinates within the protein-ligand complex, a dynamic workflow was developed. In details, molecular dynamic was used as tool to identify the most significant ligand-protein interactions from several crystallized protein structures. The identified features were used for the creation of dynamic pha…

Computer scienceAllosteric regulationBinding pocketmacromolecular substancesComputational biologyMolecular Dynamics SimulationLigands01 natural sciences03 medical and health sciencesProtein structureStructural BiologyDrug DiscoveryHumans030304 developmental biologyEED0303 health sciencesVirtual screeningBinding SitesbiologyOrganic ChemistryMolecular DynamicPolycomb Repressive Complex 2Dynamic pharmacophorePRC20104 chemical sciencesComputer Science ApplicationsChromatinMolecular Docking Simulation010404 medicinal & biomolecular chemistryROC CurveDocking (molecular)Drug Designbiology.proteinMolecular MedicinePharmacophorePRC2Allosteric SiteProtein BindingMolecular informaticsReferences
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Microseparation techniques for the study of the enantioselectivity of drug-plasma protein binding.

2009

Stereoselectivity in protein binding can have a significant effect on the pharmacokinetic and pharmacodynamic properties of chiral drugs. The investigation of enantioselectivity of drugs in their binding with human plasma proteins and the identification of the molecular mechanisms involved in the stereodiscrimination by the proteins represent a great challenge for clinical pharmacology. In this review, the separation techniques used for enantioselective protein binding experiments are described and compared. An overview of studies on enantiomer–protein interactions, enantiomer–enantiomer interactions as well as chiral drug–drug interactions, including allosteric effects, is presented. The c…

Drugmedia_common.quotation_subjectClinical BiochemistryAllosteric regulationPlasma protein bindingBiochemistryChromatography AffinityAnalytical ChemistryPharmacokineticsSpecies SpecificityDrug DiscoveryHumansAnimal speciesMolecular Biologymedia_commonPharmacologyChromatographyChemistryEnantioselective synthesisElectrophoresis CapillaryStereoisomerismGeneral MedicineBlood ProteinsBlood proteinsPharmaceutical PreparationsChromatography GelStereoselectivityAllosteric SiteProtein BindingBiomedical chromatography : BMC
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Cooperative Transition in the Conformation of 24-Mer Tarantula Hemocyanin upon Oxygen Binding

2005

Hemocyanins are large respiratory proteins of arthropods and mollusks, which bind oxygen with very high cooperativity. Here, we investigated the relationship between oxygen binding and structural changes of the 24-mer tarantula hemocyanin. Oxygen binding of the hemocyanin was detected following the fluorescence intensity of the intrinsic tryptophans. Under the same conditions, structural changes were monitored by the non-covalently bound fluorescence probe Prodan (6-propionyl-2-(dimethylamino)-naphthalene), which is very sensitive to its surroundings. Upon oxygen binding of the hemocyanin a red shift of 5 nm in the emission maximum of the label was observed. A comparison of oxygen binding c…

Macromolecular SubstancesProtein ConformationPartial Pressuremedicine.medical_treatmentAllosteric regulationMolecular ConformationAnalytical chemistrychemistry.chemical_elementchemical and pharmacologic phenomenaCooperativitycomplex mixturesBiochemistryOxygenProtein structure2-NaphthylaminemedicineAnimalsBinding siteMolecular BiologyBinding SitesChemistryTryptophanSpidersHemocyaninCell BiologyFluorescenceOxygenSpectrometry FluorescenceMicroscopy FluorescenceModels ChemicalSpectrophotometryHemocyaninsBiophysicsAllosteric SiteOxygen bindingProtein BindingJournal of Biological Chemistry
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Novel Analgesic Agents Obtained by Molecular Hybridization of Orthosteric and Allosteric Ligands

2019

AbstractDespite the high incidence of acute and chronic pain in the general population, the efficacy of currently available medications is unsatisfactory. Insufficient management of pain has a profound impact on the quality of life and can have serious physical, psychological, social, and economic consequences. This unmet need reflects a failure to develop novel classes of analgesic drugs with superior clinical properties and lower risk of abuse. Nevertheless, recent advances in our understanding of the neurobiology of pain are offering new opportunities for developing different therapeutic approaches. Among those, the activation of M2 muscarinic acetylcholine receptors, which play a key ro…

Male0301 basic medicineGuinea PigsPopulationAnalgesicAllosteric regulationPainIn Vitro TechniquesMotor ActivityLigandsBioinformaticsAnalgesic agentsMice03 medical and health sciences0302 clinical medicineAllosteric RegulationDrug DiscoveryMuscarinic acetylcholine receptormedicineAnimalsHeart AtriaeducationPharmacologyAnalgesicsReceptor Muscarinic M2education.field_of_studyBehavior AnimalDose-Response Relationship Drugbusiness.industryChronic painmedicine.diseaseMolecular hybridization030104 developmental biologyTolerabilityCholinergicAtrial Function LeftbusinessAllosteric Site030217 neurology & neurosurgery
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A lipid transfer protein binds to a receptor involved in the control of plant defence responses

2001

AbstractLipid transfer proteins (LTPs) and elicitins are both able to load and transfer lipidic molecules and share some structural and functional properties. While elicitins are known as elicitors of plant defence mechanisms, the biological function of LTP is still an enigma. We show that a wheat LTP1 binds with high affinity sites. Binding and in vivo competition experiments point out that these binding sites are common to LTP1 and elicitins and confirm that they are the biological receptors of elicitins. A mathematical analysis suggests that these receptors could be represented by an allosteric model corresponding to an oligomeric structure with four identical subunits.

Models Molecular0106 biological sciencesTime FactorsProtein ConformationPlasma protein bindingLigands01 natural sciencesBiochemistryProtein structureStructural BiologyReceptorAllosteryTriticumComputingMilieux_MISCELLANEOUSPlant Proteins0303 health sciencesFungal proteinfood and beveragesCell biologyBiochemistryPlant lipid transfer proteinsAllosteric SiteProtein BindingReceptorPhytophthoraLipid transfer proteinAllosteric regulationBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyBinding CompetitiveFungal Proteins03 medical and health sciencesTobaccoGeneticsBinding site[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular Biology030304 developmental biologyBinding SitesDose-Response Relationship DrugAlgal ProteinsCell MembraneElicitinCell BiologyAntigens PlantModels TheoreticalLipid MetabolismElicitinCarrier Proteins010606 plant biology & botanyFEBS Letters
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The Monod-Wyman-Changeux allosteric model accounts for the quaternary transition dynamics in wild type and a recombinant mutant human hemoglobin

2012

International audience; The acknowledged success of the Monod-Wyman-Changeux (MWC) allosteric model stems from its efficacy in accounting for the functional behavior of many complex proteins starting with hemoglobin (the paradigmatic case) and extending to channels and receptors. The kinetic aspects of the allosteric model, however, have been often neglected, with the exception of hemoglobin and a few other proteins where conformational relaxations can be triggered by a short and intense laser pulse, and monitored by time-resolved optical spectroscopy. Only recently the application of time-resolved wide-angle X-ray scattering (TR-WAXS), a direct structurally sensitive technique, unveiled th…

Models MolecularProtein ConformationcooperativityMESH: Catalytic DomainCooperativity01 natural sciencesMESH: Recombinant ProteinsHemoglobinsProtein structureMESH: Protein ConformationCatalytic Domainprotein structural dynamicsMESH: Allosteric Site0303 health sciencesMultidisciplinaryallosterybiologyMESH: KineticsChemistryBiological SciencesRecombinant Proteins[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsMESH: HemoglobinsAllosteric SiteMESH: Models MolecularAdultMESH: MutationStereochemistryKineticsAllosteric regulation010402 general chemistry03 medical and health sciencesprotein conformational changesflash photolysisallostery; cooperativity; flash photolysis; hemoglobin; protein conformational changes; protein structural dynamics; time-resolved wide angle x ray scattering; time-resolved x-ray scatteringHumans030304 developmental biologytime-resolved X-ray scattering; protein conformational changes; cooperativity; flash photolysisMESH: Humanstime-resolved X-ray scatteringWild typeActive sitetime-resolved wide angle x ray scatteringMESH: AdulthemoglobinSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)0104 chemical sciencesprotein conformational changeKineticsAllosteric enzymeMutationbiology.proteinHemoglobin
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Allosterically potentiating ligands of nicotinic receptors as a treatment strategy for Alzheimer's disease.

2000

Abstract One of the most prominent cholinergic deficit in Alzheimer’s disease (AD) is the reduced number of nicotinic acetylcholine receptors (nAChR) in the hippocampus and cortex of AD patients, as compared to age-matched controls. This deficit results in reduced nicotinic cholinergic excitation which may not only impair postsynaptic depolarization but also presynaptic neurotransmitter release and Ca 2+ -dependent intracellular signaling, including transcriptional activity. Presently, the most common approach to correct the nicotinic cholinergic deficit in AD is the application of cholinesterase inhibitors. Due to the resulting increase in synaptic acetylcholine levels, both in concentrati…

NeuronsPatch-Clamp TechniquesBiologyNeurotransmissionReceptors NicotinicSynaptic TransmissionCell LineBehavioral NeuroscienceNicotinic acetylcholine receptorMiceGanglion type nicotinic receptorNicotinic agonistAllosteric RegulationAlzheimer DiseaseMuscarinic acetylcholine receptormedicineAnimalsHumansNicotinic AgonistsAlpha-4 beta-2 nicotinic receptorNeuroscienceAcetylcholine5-HT receptorAllosteric Sitemedicine.drugBehavioural brain research
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Proline-Based Allosteric Inhibitors of Zika and Dengue Virus NS2B/NS3 Proteases

2019

The NS2B/NS3 serine proteases of the Zika and Dengue flaviviruses are attractive targets for the development of antiviral drugs. We report the synthesis and evaluation of a new, proline-based compound class that displays allosteric inhibition of both proteases. The structural features relevant for protease binding and inhibition were determined to establish them as new lead compounds for flaviviral inhibitors. Based on our structure-activity relationship studies, the molecules were further optimized, leading to inhibitors with submicromolar IC50 values and improved lipophilic ligand efficiency. The allosteric binding site in the proteases was probed using mutagenesis and covalent modificati…

ProteasesProlineProtein ConformationAllosteric regulationViral Nonstructural ProteinsDengue virusmedicine.disease_causeAntiviral Agents01 natural sciencesDengueSerineStructure-Activity RelationshipViral Proteins03 medical and health sciencesAllosteric RegulationCatalytic DomainDrug DiscoverymedicineHumansStructure–activity relationshipProtease Inhibitors030304 developmental biology0303 health sciencesNS3Ligand efficiencyZika Virus InfectionChemistryProtease bindingSerine EndopeptidasesZika VirusDengue Virus0104 chemical sciencesMolecular Docking Simulation010404 medicinal & biomolecular chemistryBiochemistryA549 CellsMolecular MedicineAllosteric SitePeptide HydrolasesProtein BindingJournal of Medicinal Chemistry
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In Silico Design of New Dual Inhibitors of SARS-CoV-2 MPRO through Ligand- and Structure-Based Methods

2023

The viral main protease is one of the most attractive targets among all key enzymes involved in the life cycle of SARS-CoV-2. Considering its mechanism of action, both the catalytic and dimerization regions could represent crucial sites for modulating its activity. Dual-binding the SARS-CoV-2 main protease inhibitors could arrest the replication process of the virus by simultaneously preventing dimerization and proteolytic activity. To this aim, in the present work, we identified two series’ of small molecules with a significant affinity for SARS-CoV-2 MPRO, by a hybrid virtual screening protocol, combining ligand- and structure-based approaches with multivariate statistical analysis. The B…

SARS-CoV-2 MPROOrganic Chemistrycatalytic site; allosteric site; SARS-CoV-2 M<sup>PRO</sup>; inhibitors; benzo[<i>b</i>]thiophene; benzo[<i>b</i>]furan; dual binding site activitiesGeneral Medicinecatalytic siteSettore CHIM/08 - Chimica FarmaceuticaCatalysisComputer Science ApplicationsInorganic Chemistrybenzo[b]furaninhibitorsbenzo[b]thiophenedual binding site activitiesallosteric sitePhysical and Theoretical ChemistryMolecular BiologySpectroscopyInternational Journal of Molecular Sciences
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