Search results for "Fluorescence resonance energy transfer"

showing 10 items of 61 documents

Discovery and structure-activity relationship studies of irreversible benzisothiazolinone-based inhibitors against Staphylococcus aureus sortase A tr…

2014

Gram-positive bacteria, in general, and staphylococci, in particular, are the widespread cause of nosocomial and community-acquired infections. The rapid evolvement of strains resistant to antibiotics currently in use is a serious challenge. Novel antimicrobial compounds have to be developed to fight these resistant bacteria, and sortase A, a bacterial cell wall enzyme, is a promising target for novel therapies. As a transpeptidase that covalently attaches various virulence factors to the cell surface, this enzyme plays a crucial role in the ability of bacteria to invade the host's tissues and to escape the immune response. In this study we have screened a small molecule library against rec…

Staphylococcus aureusClinical BiochemistryPharmaceutical ScienceVirulenceStaphylococcal infectionsmedicine.disease_causeBiochemistryBacterial cell structureMicrobiologyStructure-Activity RelationshipBacterial ProteinsSortaseDrug DiscoverymedicineFluorescence Resonance Energy TransferHumansEnzyme InhibitorsMolecular BiologybiologyChemistryOrganic ChemistryStaphylococcal InfectionsAntimicrobialmedicine.diseasebiology.organism_classificationAminoacyltransferasesHigh-Throughput Screening AssaysMolecular Docking SimulationCysteine EndopeptidasesThiazolesBiochemistryStaphylococcus aureusSortase AMolecular MedicineBacteriaBioorganicmedicinal chemistry
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Visualization of RNA-Quadruplexes in Live Cells

2015

Visualization of DNA and RNA quadruplex formation in human cells was demonstrated recently with different quadruplex-specific antibodies. Despite the significant interest in these immunodetection approaches, dynamic detection of quadruplex in live cells remains elusive. Here, we report on NaphthoTASQ (N-TASQ), a next-generation quadruplex ligand that acts as a multiphoton turn-on fluorescent probe. Single-step incubation of human and mouse cells with N-TASQ enables the direct detection of RNA-quadruplexes in untreated cells (no fixation, permeabilization or mounting steps), thus offering a unique, unbiased visualization of quadruplexes in live cells.

Static ElectricityMelanoma ExperimentalLigands010402 general chemistryG-quadruplex01 natural sciencesBiochemistryCatalysisMice03 medical and health scienceschemistry.chemical_compoundColloid and Surface ChemistryBiomimeticsCationsCell Line TumorFluorescence Resonance Energy TransferAnimalsHumans[CHIM]Chemical Sciences[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biologyheterocyclic compoundsComputingMilieux_MISCELLANEOUSChelating AgentsFluorescent Dyes030304 developmental biologyPhotons[SDV.GEN]Life Sciences [q-bio]/Genetics0303 health sciencesbiologyChemistryRNADNAGeneral ChemistryFluorescenceMolecular biology3. Good health0104 chemical sciencesCell biologyVisualizationG-QuadruplexesFörster resonance energy transferMicroscopy FluorescenceCell cultureMCF-7 Cellsbiology.proteinRNAAntibodyDNAJournal of the American Chemical Society
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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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The oxidation state of a protein observed molecole-by-molecule.

2005

We report the observation of the redox state of the blue copper protein azurin on the single-molecule level. The fluorescence of a small fluorophore attached to the protein is modulated by the change in absorption of the copper center via fluorescence resonance energy transfer (FRET). In our model system, the fluorescence label Cy5 was coupled to azurin from Pseudomonas aeruginosa via cysteine K27C. The Cy5 fluorescence was partially quenched by the absorption of the copper center of azurin in its oxidized state. In the reduced state, absorption is negligible, and thus no quenching occurs. We report on single-molecule measurements, both in solution by using fluorescence correlation spectros…

Surface PropertiesChemistryFluorescence spectrometryFluorescence correlation spectroscopyCarbocyaninesFluorescence in the life sciencesPhotochemistrySensitivity and SpecificityFluorescenceAtomic and Molecular Physics and OpticsFluorescence spectroscopyAbsorptionSpectrometry FluorescenceResonance fluorescenceAzurinPseudomonas aeruginosaFluorescence Resonance Energy TransferFluorescence cross-correlation spectroscopyPhysical and Theoretical ChemistryAzurinOxidation-ReductionCopperFluorescent Dyes
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Cholesterol Modulates the Interaction of β-Amyloid Peptide with Lipid Bilayers

2009

The interaction of an amphiphilic, 40-amino acid beta-amyloid (Abeta) peptide with liposomal membranes as a function of sterol mole fraction (X(sterol)) was studied based on the fluorescence anisotropy of a site-specific membrane sterol probe, dehydroergosterol (DHE), and fluorescence resonance energy transfer (FRET) from the native Tyr-10 residue of Abeta to DHE. Without Abeta, peaks or kinks in the DHE anisotropy versus X(sterol) plot were detected at X(sterol) approximately 0.25, 0.33, and 0.53. Monomeric Abeta preserved these peaks/kinks, but oligomeric Abeta suppressed them and created a new DHE anisotropy peak at X(sterol) approximately 0.38. The above critical X(sterol) values coinci…

Time FactorsLipid BilayersMolecular Sequence DataBiophysicsPeptideFluorescence Polarization7. Clean energy03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAlzheimer DiseaseErgosterolFluorescence Resonance Energy TransferAmino Acid SequenceLipid bilayer030304 developmental biologychemistry.chemical_classification0303 health sciencesLiposomeAmyloid beta-PeptidesChemistryCholesterolSterolPeptide FragmentsCrystallographyFörster resonance energy transferMembraneCholesterolCell BiophysicsTyrosinelipids (amino acids peptides and proteins)030217 neurology & neurosurgeryFluorescence anisotropyProtein BindingBiophysical Journal
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Kondrat'eva ligation: Diels-Alder-based irreversible reaction for bioconjugation.

2014

International audience; Diversification of existing chemoselective ligations is required to efficiently access complex and well-defined biomolecular assemblies with unique and valuable properties. The development and bioconjugation applications of a novel Diels-Alder-based irreversible site-specific ligation are reported. The strategy is based on a Kondrat'eva cycloaddition between bioinert and readily functionalizable 5-alkoxyoxazoles and maleimides that readily react together under mild and easily tunable reaction conditions to afford a fully stable pyridine scaffold. The potential of this novel bioconjugation is demonstrated through the preparation of fluorescent conjugates of biomolecul…

[CHIM.THER]Chemical Sciences/Medicinal ChemistryLigandsCatalysis[CHIM.ANAL]Chemical Sciences/Analytical chemistryFluorescence Resonance Energy TransferOrganic chemistryNuclear Magnetic Resonance BiomolecularOxazoleschemistry.chemical_classificationBioconjugationCycloaddition ReactionMolecular Structure[CHIM.ORGA]Chemical Sciences/Organic chemistryChemistryBiomoleculeOrganic Chemistry[CHIM.CATA]Chemical Sciences/CatalysisFluorescenceUrokinase-Type Plasminogen ActivatorCycloaddition[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryEnzyme ActivationFörster resonance energy transferLigationPlasminogen activator[CHIM.CHEM]Chemical Sciences/CheminformaticsConjugateThe Journal of organic chemistry
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Cluster dirhenium(III) cis-dicarboxylates with α-amino acids ligands as mighty selective G4s binders.

2021

The synthesis of four dirhenium(III) cis-dicarboxylates with the α-amino acids residues Asp (I), Glu (II), Phe (III) and Tyr (IV) is presented. The G-quadruplex stabilization potential was evaluated by fluorescence resonance energy transfer - melting analysis. All derivatives show specific binding to c-kit1 quadruplex, while II and IV have also strong stabilization activity to HTelo21 quadruplex. At the same time, the compounds do not show any stabilization activity for ds26 DNA, which suggests unique mechanisms of molecular DNA recognition for these complexes.

chemistry.chemical_classificationMolecular StructureStereochemistrychemistry.chemical_elementDNARheniumG-quadruplexLigandsBiochemistryAmino acidInorganic ChemistryG-Quadruplexeschemistry.chemical_compoundFörster resonance energy transferRheniumchemistryCoordination ComplexesCluster (physics)Fluorescence Resonance Energy TransferHumansheterocyclic compoundsAmino AcidsDNADna recognitionJournal of inorganic biochemistry
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Comparative analysis of the coordinated motion of Hsp70s from different organelles observed by single-molecule three-color FRET.

2021

Cellular function depends on the correct folding of proteins inside the cell. Heat-shock proteins 70 (Hsp70s), being among the first molecular chaperones binding to nascently translated proteins, aid in protein folding and transport. They undergo large, coordinated intra- and interdomain structural rearrangements mediated by allosteric interactions. Here, we applied a three-color single-molecule Forster resonance energy transfer (FRET) combined with three-color photon distribution analysis to compare the conformational cycle of the Hsp70 chaperones DnaK, Ssc1, and BiP. By capturing three distances simultaneously, we can identify coordinated structural changes during the functional cycle. Be…

chemistry.chemical_classificationOrganellesMultidisciplinarySaccharomyces cerevisiae ProteinsAllosteric regulationPeptideSaccharomyces cerevisiaeBiological SciencesMitochondrial Membrane Transport ProteinsRecombinant ProteinsSingle Molecule ImagingFolding (chemistry)Förster resonance energy transferchemistryHeat shock proteinBiophysicsEscherichia coliFluorescence Resonance Energy TransferMoleculeProtein foldingNucleotideHSP70 Heat-Shock ProteinsMolecular ChaperonesProceedings of the National Academy of Sciences of the United States of America
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Reconfigurable DNA Origami Nanocapsule for pH-Controlled Encapsulation and Display of Cargo

2019

DNA nanotechnology provides a toolbox for creating custom and precise nanostructures with nanometer-level accuracy. These nano-objects are often static by nature and serve as versatile templates for assembling various molecular components in a user-defined way. In addition to the static structures, the intrinsic programmability of DNA nanostructures allows the design of dynamic devices that can perform predefined tasks when triggered with external stimuli, such as drug delivery vehicles whose cargo display or release can be triggered with a specified physical or chemical cue in the biological environment. Here, we present a DNA origami nanocapsule that can be loaded with cargo and reversibl…

entsyymitMaterials scienceta221enzymesMetal NanoparticlesGeneral Physics and AstronomyNanoparticleNanotechnology02 engineering and technology010402 general chemistry01 natural sciencesArticleBiophysical PhenomenaNanocapsulesDrug Delivery SystemsNanocapsulesDNA nanotechnologyFluorescence Resonance Energy TransferDNA origamiDNA nanotechnologyGeneral Materials ScienceA-DNApH controlGeneral EngineeringnanobiotekniikkaDNAHydrogen-Ion Concentration021001 nanoscience & nanotechnologyNanostructures0104 chemical sciencesFörster resonance energy transferTemplateFörster resonance energy transferdrug deliveryDrug deliveryNucleic Acid ConformationnanohiukkasetnanoparticlesGoldDNA origami0210 nano-technologyACS Nano
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Nitrated Fatty Acids Modulate the Physical Properties of Model Membranes and the Structure of Transmembrane Proteins

2017

Nitrated fatty acids (NO2 -FAs) act as anti-inflammatory signal mediators, albeit the molecular mechanisms behind NO2 -FAs' influence on diverse metabolic and signaling pathways in inflamed tissues are essentially elusive. Here, we combine fluorescence measurements with surface-specific sum frequency generation vibrational spectroscopy and coarse-grained computer simulations to demonstrate that NO2 -FAs alter lipid organization by accumulation at the membrane-water interface. As the function of membrane proteins strongly depends on both, protein structure as well as membrane properties, we consecutively follow the structural dynamics of an integral membrane protein in presence of NO2 -FAs. …

inorganic chemicals0301 basic medicineProtein Conformationcomplex mixturesPhase TransitionCatalysisPhysical Phenomena03 medical and health sciences0302 clinical medicineProtein structureJournal ArticleFluorescence Resonance Energy TransferMembrane fluidityComputer SimulationLipid bilayerIntegral membrane proteinNitratesChemistryCircular DichroismCell MembraneFatty AcidsOrganic ChemistryPeripheral membrane proteinMembrane ProteinsGeneral Chemistryrespiratory systemLipidsTransmembrane protein030104 developmental biologyMembraneMembrane proteinBiochemistryBiophysics030217 neurology & neurosurgerySignal TransductionChemistry – A European Journal
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