Search results for "Mod"

showing 10 items of 39605 documents

Addition of thiols to the double bond of dipeptide C-terminal dehydroalanine as a source of new inhibitors of cathepsin C.

2017

Addition of thiols to double bond of glycyl-dehydroalanine and phenyl-dehydroalanine esters provided micromolar inhibitors of cathepsin C. The structure-activity studies indicated that dipeptides containing N-terminal phenylalanine exhibit higher affinity towards the enzyme. A series of C-terminal S-substituted cysteines are responsible for varying interaction with S1 binding pocket of cathepsin C. Depending on diastereomer these compounds most likely act as slowly reacting substrates or competitive inhibitors. This was proved by TLC analysis of the medium in which interaction of methyl (S)-phenylalanyl-(R,S)-(S-adamantyl)cysteinate (7i) with the enzyme was studied. Molecular modeling enabl…

0301 basic medicineModels MolecularDouble bondStereochemistryPhenylalanineCysteine Proteinase InhibitorsBiochemistryCathepsin CCathepsin CSubstrate Specificity03 medical and health scienceschemistry.chemical_compoundStructure-Activity Relationship0302 clinical medicineDehydroalanineMoietyAnimalsSulfhydryl CompoundsBinding sitechemistry.chemical_classificationDipeptideAlanineBinding SitesDehydropeptidesDiastereomerEnzyme inhibitorsGeneral MedicineDipeptidesKinetics030104 developmental biologychemistryThiol addition030220 oncology & carcinogenesisCattleBiochimie
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Incorporation of mRNA in Lamellar Lipid Matrices for Parenteral Administration

2018

Molecular pharmaceutics 15(2), 642 - 651 (2018). doi:10.1021/acs.molpharmaceut.7b01022

0301 basic medicineModels MolecularDrug CompoundingKineticsLipid BilayersPharmaceutical Science610TransfectionCell LineMyoblasts03 medical and health sciencesMiceX-Ray DiffractionCationsDrug DiscoveryScattering Small AngleAnimalsRNA Messengerddc:610Lipid bilayerLuciferasesMessenger RNALiposomeDrug CarriersChemistryAqueous two-phase systemRNATransfection030104 developmental biologyDelayed-Action PreparationsLiposomesBiophysicsMolecular Medicinelipids (amino acids peptides and proteins)Drug carrier
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Probing Differential Binding Mechanisms of Phenylalanine-Glycine-Rich Nucleoporins by Single-Molecule FRET

2018

Abstract Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex. They are highly dynamic under physiological conditions and studying their interaction with nuclear transport receptors (NTRs) is key to understanding the molecular mechanism of nucleocytoplasmic transport. Distinct conformational features of FG-Nups interacting with diverse NTRs can be detected by multiparameter single-molecule fluorescence energy transfer (smFRET), which is a powerful technique for studying the dynamics and interactions of biomolecules in solution. Here we provide a detailed protocol utilizing smFRET to reveal dif…

0301 basic medicineModels MolecularGlycosylationProtein ConformationPhenylalanineGlycineIntrinsically disordered proteinsArticle03 medical and health scienceschemistry.chemical_compoundFluorescence Resonance Energy TransferAnimalsHumansNuclear porechemistry.chemical_classificationBiomoleculeSingle-molecule FRETEquipment DesignIntrinsically Disordered ProteinsNuclear Pore Complex Proteins030104 developmental biologychemistryNucleocytoplasmic TransportBiophysicsNucleoporinNuclear transportProtein BindingIntrinsically Disordered Proteins
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Two differential binding mechanisms of FG-nucleoporins and nuclear transport receptors

2018

Summary Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex (NPC). Previous studies showed that nuclear transport receptors (NTRs) were found to interact with FG-Nups by forming an “archetypal-fuzzy” complex through the rapid formation and breakage of interactions with many individual FG motifs. Here, we use single-molecule studies combined with atomistic simulations to show that, in sharp contrast, FG-Nup214 undergoes a coupled reconfiguration-binding mechanism when interacting with the export receptor CRM1. Association and dissociation rate constants are more than an order of magnitude lowe…

0301 basic medicineModels MolecularGlycosylationglycosylationProtein ConformationPhenylalanineGlycineSequence (biology)Intrinsically disordered proteinsnuclear transport receptorssingle-molecule FRETGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health scienceschemistry.chemical_compound0302 clinical medicineEscherichia coliFluorescence Resonance Energy TransferHumansNuclear poreReceptorlcsh:QH301-705.5Single-molecule FRETmolecular dynamics simulationsbinding mechanismintrinsically disordered proteinFG-Nup3. Good healthNuclear Pore Complex Proteins030104 developmental biologychemistrylcsh:Biology (General)BiophysicsNuclear PoreNucleoporinNuclear transport030217 neurology & neurosurgeryProtein BindingCell Reports
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Prefolded Synthetic G-Quartets Display Enhanced Bioinspired Properties

2016

International audience; A water-soluble template-assembled synthetic G-quartet (TASQ) based on the use of a macrocyclodecapeptide scaffold was designed to display stable intramolecular folds alone in solution. The preformation of the guanine quartet, demonstrated by NMR and CD investigations, results in enhanced peroxidase-type biocatalytic activities and improved quadruplex-interacting properties. Comparison of its DNAzyme-boosting properties with the ones of previously published TASQ revealed that, nowadays, it is the best DNAzyme-boosting agent.

0301 basic medicineModels MolecularGuanineStereochemistryDNAzymewaterSupramolecular chemistryDeoxyribozymednainsights010402 general chemistryG-QuartetsG-quadruplexchemistry[ CHIM ] Chemical Sciences01 natural sciencesCatalysissupramolecular chemistryg-quadruplex structures03 medical and health scienceschemistry.chemical_compoundG-quartets[CHIM]Chemical SciencesrnaComputingMilieux_MISCELLANEOUSligandsbiologyOrganic Chemistry[CHIM.CATA]Chemical Sciences/CatalysisGeneral ChemistryDNA CatalyticSmall moleculeG-quadruplexes0104 chemical sciencesSolutionssmall molecules030104 developmental biologychemistryBiocatalysisIntramolecular forceBiocatalysisNucleic Acid Conformationcyclodecapeptideacid
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Sensory domain contraction in histidine kinase CitA triggers transmembrane signaling in the membrane-bound sensor

2017

Bacteria use membrane-integral sensor histidine kinases (HK) to perceive stimuli and transduce signals from the environment to the cytosol. Information on how the signal is transmitted across the membrane by HKs is still scarce. Combining both liquid- and solid-state NMR, we demonstrate that structural rearrangements in the extracytoplasmic, citrate-sensing Per-Arnt-Sim (PAS) domain of HK CitA are identical for the isolated domain in solution and in a longer construct containing the membrane-embedded HK and lacking only the kinase core. We show that upon citrate binding, the PAS domain contracts, resulting in a shortening of the C-terminal β-strand. We demonstrate that this contraction of t…

0301 basic medicineModels MolecularHistidine Kinase030106 microbiologyMolecular ConformationCitric Acid03 medical and health sciencesStructure-Activity RelationshipBacterial ProteinsPAS domainProtein Interaction Domains and MotifsAmino Acid SequenceHistidineMultidisciplinaryChemistryKinaseHistidine kinaseGeobacillusMembrane ProteinsBiological SciencesTransmembrane proteinCell biologyCytosolHelixSignal transductionProtein BindingSignal Transduction
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Recombinant anthrax protective antigen: Observation of aggregation phenomena by TEM reveals specific effects of sterols.

2017

Abstract Negatively stained transmission electron microscope images are presented that depict the aggregation of recombinant anthrax protective antigen (rPA83 monomer and the PA63 prepore oligomer) under varying in vitro biochemical conditions. Heat treatment (50 °C) of rPA83 produced clumped fibrils, but following heating the PA63 prepore formed disordered aggregates. Freeze-thaw treatment of the PA63 prepore generated linear flexuous aggregates of the heptameric oligomers. Aqueous suspensions of cholesterol microcrystals were shown to bind small rPA83 aggregates at the edges of the planar bilayers. With PA63 a more discrete binding of the prepores to the crystalline cholesterol bilayer ed…

0301 basic medicineModels MolecularHot TemperatureBacterial ToxinsGeneral Physics and AstronomyFibrilOligomerNegative Staining03 medical and health scienceschemistry.chemical_compoundProtein AggregatesMicroscopy Electron TransmissionStructural BiologyFreezingGeneral Materials ScienceAntigens BacterialAqueous solutionChemistryBilayerCell BiologyHydrogen-Ion ConcentrationNegative stainSterolRecombinant ProteinsCrystallographySterols030104 developmental biologyMonomerCholesterolTransmission electron microscopyCrystallizationDeoxycholic AcidMicron (Oxford, England : 1993)
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Oncogenic Deregulation of EZH2 as an Opportunity for Targeted Therapy in Lung Cancer.

2016

Abstract As a master regulator of chromatin function, the lysine methyltransferase EZH2 orchestrates transcriptional silencing of developmental gene networks. Overexpression of EZH2 is commonly observed in human epithelial cancers, such as non–small cell lung carcinoma (NSCLC), yet definitive demonstration of malignant transformation by deregulated EZH2 remains elusive. Here, we demonstrate the causal role of EZH2 overexpression in NSCLC with new genetically engineered mouse models of lung adenocarcinoma. Deregulated EZH2 silences normal developmental pathways, leading to epigenetic transformation independent of canonical growth factor pathway activation. As such, tumors feature a transcrip…

0301 basic medicineModels MolecularLung Neoplasmsmedicine.medical_treatmentMolecular ConformationGene ExpressionAntineoplastic Agentsmacromolecular substancesBiologymedicine.disease_causeArticleMalignant transformationTargeted therapy03 medical and health sciencesMiceStructure-Activity RelationshipCell Line TumormedicineAnimalsHumansEnhancer of Zeste Homolog 2 ProteinMolecular Targeted TherapyLung cancerPromoter Regions GeneticGene Expression ProfilingEZH2Cancermedicine.diseaseMagnetic Resonance ImagingXenograft Model Antitumor AssaysChromatinrespiratory tract diseasesGene Expression Regulation NeoplasticDisease Models Animal030104 developmental biologyCell Transformation NeoplasticEnhancer Elements GeneticOncologyDrug DesignCancer researchAdenocarcinomaKRASEpigenetic therapyCancer discovery
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rbFOX1/MBNL1 competition for CCUG RNA repeats binding contributes to myotonic dystrophy type 1/type 2 differences

2018

Myotonic dystrophy type 1 and type 2 (DM1, DM2) are caused by expansions of CTG and CCTG repeats, respectively. RNAs containing expanded CUG or CCUG repeats interfere with the metabolism of other RNAs through titration of the Muscleblind-like (MBNL) RNA binding proteins. DM2 follows a more favorable clinical course than DM1, suggesting that specific modifiers may modulate DM severity. Here, we report that the rbFOX1 RNA binding protein binds to expanded CCUG RNA repeats, but not to expanded CUG RNA repeats. Interestingly, rbFOX1 competes with MBNL1 for binding to CCUG expanded repeats and overexpression of rbFOX1 partly releases MBNL1 from sequestration within CCUG RNA foci in DM2 muscle ce…

0301 basic medicineModels MolecularProtein Conformation alpha-Helical[SDV]Life Sciences [q-bio]General Physics and AstronomyGene ExpressionRNA-binding proteinCrystallography X-Raychemistry.chemical_compoundMOLECULAR-BASISGene expressionMBNL1Myotonic DystrophyComputingMilieux_MISCELLANEOUSMultidisciplinaryCHLORIDE CHANNELQRNA-Binding ProteinsRecombinant Proteins3. Good healthCell biologyCONGENITAL HEART-DISEASEDrosophila melanogasterThermodynamicsSKELETAL-MUSCLERNA Splicing FactorsCUG REPEATSProtein BindingRNA Splicing Factorsmusculoskeletal diseasesSTEADY-STATEcongenital hereditary and neonatal diseases and abnormalitiesScienceRBFOX1BiologyMyotonic dystrophyBinding CompetitiveGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesmedicineEscherichia coliAnimalsHumansProtein Interaction Domains and MotifsBinding siteNucleotide MotifsMuscle SkeletalSPLICING REGULATOR RBFOX2MUSCLEBLIND PROTEINSBinding SitesPRE-MESSENGER-RNARNAGeneral Chemistrymedicine.diseaseDisease Models AnimalKinetics030104 developmental biologychemistryTRIPLET REPEATRNAProtein Conformation beta-Strand3111 Biomedicine
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Bioactive triterpenes of protium heptaphyllum gum resin extract display cholesterol-lowering potential

2021

Hypercholesterolemia is one of the major causes of cardiovascular disease, the risk of which is further increased if other forms of dyslipidemia occur. Current therapeutic strategies include changes in lifestyle coupled with drug administration. Statins represent the most common therapeutic approach, but they may be insufficient due to the onset of resistance mechanisms and side effects. Consequently, patients with mild hypercholesterolemia prefer the use of food supplements since these are perceived to be safer. Here, we investigate the phytochemical profile and cholesterol-lowering potential of Protium heptaphyllum gum resin extract (PHE). Chemical characterization via HPLC-APCI-HRMS2 and…

0301 basic medicineModels MolecularProtein ConformationDrug Evaluation Preclinical030204 cardiovascular system & hematologyPharmacologyPPARαTerpenelcsh:ChemistryPCSK9chemistry.chemical_compound0302 clinical medicineCatalytic DomainSettore BIO/10 - BiochimicaPlant Gumslcsh:QH301-705.5SpectroscopyChromatography High Pressure LiquidFlame IonizationMonacolinChemistryAnticholesteremic AgentsGeneral MedicineComputer Science ApplicationsMolecular Docking SimulationCholesterolPhytochemicalMolecular dockinglipids (amino acids peptides and proteins)Breu brancoStatinmedicine.drug_classHypercholesterolemiaArticleCatalysisGas Chromatography-Mass SpectrometryInorganic Chemistry03 medical and health sciencesNutraceuticalmedicineHumansLovastatinPhysical and Theoretical ChemistryMolecular BiologyOleananeHMGCREnzymatic activityCholesterolPCSK9Organic ChemistryStatinSettore CHIM/08 - Chimica FarmaceuticaTriterpenes030104 developmental biologyhypercholesterolemia; gene expression; HMGCR; PCSK9; PPARα; enzymatic activity; molecular docking; statin; monacolin; breu brancolcsh:Biology (General)lcsh:QD1-999Breu branco; Enzymatic activity; Gene expression; HMGCR; Hypercholesterolemia; Molecular docking; Monacolin; PCSK9; PPARα; StatinLDL receptorDietary SupplementsHepatocytesSettore BIO/14 - FarmacologiaGene expressionHydroxymethylglutaryl-CoA Reductase InhibitorsResins PlantHydrogen
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