Search results for "dichroism"

showing 10 items of 471 documents

Specific and highly efficient condensation of GC and IC DNA by polyaza pyridinophane derivatives

2018

Abstract Two bis-polyaza pyridinophane derivatives and their monomeric reference compounds revealed strong interactions with ds-DNA and RNA. The bis-derivatives show a specific condensation of GC- and IC-DNA, which is almost two orders of magnitude more efficient than the well-known condensation agent spermine. The type of condensed DNA was identified as ψ-DNA, characterized by the exceptionally strong CD signals. At variance to the almost silent AT(U) polynucleotides, these strong CD signals allow the determination of GC-condensates at nanomolar nucleobase concentrations. Detailed thermodynamic characterisation by ITC reveals significant differences between the DNA binding of the bis-deriv…

0301 basic medicineCircular dichroismStereochemistryPyridonesEnthalpySpermineCalorimetryMicroscopy Atomic ForceNucleic Acid DenaturationBiochemistryNucleobase03 medical and health scienceschemistry.chemical_compoundStructural BiologyPyridinophane compounds ; DNA/RNA binding ; GC-DNA condensation ; circular dichroism spectroscopyMolecular BiologyRNA Double-StrandedAnalytic ChemistryCircular DichroismOrganic ChemistryTemperatureRNAGeneral MedicineDNAChemistry030104 developmental biologyMonomerchemistryPolynucleotideNucleic Acid ConformationDNA
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Aza-macrocyclic triphenylamine ligands for G-quadruplex recognition

2018

A new series of triphenylamine-based ligands with one (TPA1PY), two (TPA2PY) or three pendant aza-macrocycle(s) (TPA3PY) has been synthesised and studied by means of pH-metric titrations, UV/Vis spectroscopy and fluorescence experiments. The affinity of these ligands for G-quadruplex (G4) DNA and the selectivity they show for G4s over duplex DNA were investigated by Forster resonance energy transfer (FRET) melting assays, fluorimetric titrations and circular dichroism spectroscopy. Interestingly, the interactions of the bi- and especially the tri-branched ligands with G4s lead to a very intense redshifted fluorescence emission band that may be associated with intermolecular aggregation betw…

0301 basic medicineCircular dichroismaggregation-induced emissionChemistry Multidisciplinaryamines010402 general chemistryG-quadruplexTriphenylamine01 natural sciencesCatalysisCIRCULAR-DICHROISM03 medical and health scienceschemistry.chemical_compoundGeneral chemistryfluorescent probestriphenylamine polyaminesMoleculeSpectroscopyFLUORESCENT-PROBESScience & TechnologyG-quadruplexChemistryINTRAMOLECULAR CHARGE-TRANSFERANTICANCER DRUG DESIGNOrganic ChemistryaggregationFORMING REGIONDNAGeneral ChemistryFluorescenceG-quadruplexes0104 chemical sciencesCrystallographyChemistry030104 developmental biologyFörster resonance energy transfer2-PHOTON ABSORPTIONPROMOTER REGIONPhysical SciencesEQUILIBRIUM-CONSTANTSGRAPHENE OXIDE03 Chemical Sciencesmacrocyclic ligands
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Biophysical and functional characterization of the human olfactory receptor OR1A1 expressed in a mammalian inducible cell line

2014

International audience; Olfactory receptors (ORs) play a crucial role in detecting the odorant molecules present in the surrounding environment. These receptors, which belong to class A G-protein-coupled receptors, constitute the largest transmembrane protein family in the human genome. Functional studies showed that the OR family includes members that are able to respond to a large set of odorants and members that are activated by a relatively small number of related odorants. To understand the molecular mechanisms that govern the receptor-ligand interactions, we overexpressed the human OR hOR1A1 in a stable tetracycline-inducible HEK293S cell line. This receptor was engineered by insertin…

0301 basic medicineCircular dichroismbindingpurification[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process Engineering[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionRecombinant Fusion ProteinsGene Expressionodorant receptorsBiologyReceptors OdorantEpitope03 medical and health sciencesRecombinant expression[SDV.IDA]Life Sciences [q-bio]/Food engineeringmedicineOlfactory receptorHumans[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringReceptorSite-directed mutagenesisagonistLigand bindingComputingMilieux_MISCELLANEOUSbeta(2)-adrenergic receptorOlfactory receptortechnology industry and agricultureStructure[SDV.IDA] Life Sciences [q-bio]/Food engineeringTransmembrane proteinprotein-coupled receptors[SDV.AEN] Life Sciences [q-bio]/Food and Nutrition030104 developmental biologymedicine.anatomical_structureHEK293 CellsBiochemistryCell culturehigh-level expressionmembrane-proteinsBeta-2 adrenergic receptoractivationsite-directed mutagenesis[SDV.AEN]Life Sciences [q-bio]/Food and NutritionBiotechnology
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Effect of high pressure on the antimicrobial activity and secondary structure of the bacteriocin nisin

2018

International audience; Effect of high pressure (HP) treatment on the antimicrobial properties and the structure of nisin was evaluated. Nisin solutions at pH 2.8 or 6.1 were treated by HP at 500 MPa – 10 min – 20 °C and their antimicrobial potency was determined. It appeared that HP clearly impacted the antimicrobial activity of nisin, with respective activity loss of 22.5% and 49.9% at pH 2.8 and 6.1. Structural analysis of nisin by circular dichroism and Fourier transform-infrared spectroscopies revealed that the decrease of nisin antimicrobial activity was likely due to the unfolding of the protein induced by HP. A loss of nisin β-turns structure, particularly significant at neutral pH,…

0301 basic medicineCircular dichroismfood.ingredient030106 microbiologyIndustrial and Manufacturing Engineering03 medical and health scienceschemistry.chemical_compound0404 agricultural biotechnologyfoodBacteriocinSecondary structure[SDV.IDA]Life Sciences [q-bio]/Food engineeringpolycyclic compoundsPotencyFood scienceProtein secondary structureNisinNisinbiologyFood additive[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringfood and beverages04 agricultural and veterinary sciencesGeneral Chemistrybiochemical phenomena metabolism and nutritionAntimicrobialbiology.organism_classification040401 food scienceActivityHigh pressurechemistrybacterialipids (amino acids peptides and proteins)BacteriaFood Science
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Direct observation of alpha-lactalbumin, adsorption and incorporation into lipid membrane and formation of lipid/protein hybrid structures

2019

The interaction between proteins and membranes is of great interest in biomedical and biotechnological research for its implication in many functional and dysfunctional processes. We present an experimental study on the interaction between model membranes and alpha-lactalbumin (alpha-La). alpha-La is widely studied for both its biological function and its anti-tumoral properties. We use advanced fluorescence microscopy and spectroscopy techniques to characterize alpha-La-membrane mechanisms of interaction and alpha-La-induced modifications of membranes when insertion of partially disordered regions of protein chains in the lipid bilayer is favored. Moreover, using fluorescence lifetime imag…

0301 basic medicineFluorescence-lifetime imaging microscopyProtein ConformationLipid BilayersBiophysics02 engineering and technologyBiochemistryMembrane Lipids03 medical and health sciencesProtein structureMembrane fluidityFluorescence microscopeAnimalsHumansLipid bilayerMolecular BiologyFluorescent DyesChemistryMembrane structure021001 nanoscience & nanotechnologyLipids2-PHOTON FLUORESCENCE MICROSCOPY; MOLTEN GLOBULE STATE; PARTIALLY FOLDED CONFORMATIONS; PROTEIN INTERACTIONS; CIRCULAR-DICHROISM; AMPHITROPIC PROTEINS; AMYLOID AGGREGATION; PHASOR APPROACH; OLEIC-ACID; LAURDANSpectrometry Fluorescence030104 developmental biologyMembranefluorescence FLIM Protein membrane interaction IDPLactalbuminBiophysicsCattleAdsorption0210 nano-technologyProtein adsorptionBiochimica et Biophysica Acta (BBA) - General Subjects
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High-Pressure-Driven Reversible Dissociation of α-Synuclein Fibrils Reveals Structural Hierarchy

2017

The analysis of the α-synuclein (aS) aggregation process, which is involved in Parkinson's disease etiopathogenesis, and of the structural feature of the resulting amyloid fibrils may shed light on the relationship between the structure of aS aggregates and their toxicity. This may be considered a paradigm of the ground work needed to tackle the molecular basis of all the protein-aggregation-related diseases. With this aim, we used chemical and physical dissociation methods to explore the structural organization of wild-type aS fibrils. High pressure (in the kbar range) and alkaline pH were used to disassemble fibrils to collect information on the hierarchic pathway by which distinct β-sh…

0301 basic medicineModels MolecularCircular dichroismAmyloidProtein FoldingProtein domainBeta sheetBiophysicsFibrilMicroscopy Atomic ForceSpectrum Analysis RamanDissociation (chemistry)03 medical and health sciences0302 clinical medicineProtein structureMicroscopy Electron TransmissionProtein DomainsSpectroscopy Fourier Transform InfraredEscherichia coliPressureChemistryCircular DichroismEnergy landscapeProteinsalpha synuclein amyloid recombinant proteinHydrogen-Ion ConcentrationRecombinant ProteinsCrystallography030104 developmental biologyMutationalpha-SynucleinProtein foldingProtein Conformation beta-StrandProtein Multimerization030217 neurology & neurosurgery
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Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions.

2016

Lunasin is a 43 amino acid peptide with anti-cancer, antioxidant, anti-inflammatory and cholesterol-lowering properties. Although the mechanism of action of lunasin has been characterized to some extent, its exact three-dimensional structure as well as the function of the N-terminal sequence remains unknown. We established a novel method for the production of recombinant lunasin that allows efficient isotope labeling for NMR studies. Initial studies showed that lunasin can exist in a reduced or oxidized state with an intramolecular disulfide bond depending on solution conditions. The structure of both forms of the peptide at pH 3.5 and 6.5 was characterized by CD spectroscopy and multidimen…

0301 basic medicineProtein Conformation alpha-HelicalCircular dichroismPhysiologyBeta sheetPeptideIntrinsically disordered proteinsBiochemistryLunasinAntioxidantsHistones03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineEndocrinologyNeoplasmsAnticarcinogenic AgentsHumansAmino Acid SequenceDisulfidesProtein secondary structureNuclear Magnetic Resonance BiomolecularPlant Proteinschemistry.chemical_classificationChemistryAcetylationNuclear magnetic resonance spectroscopyIntrinsically Disordered Proteins030104 developmental biologyBiochemistry030220 oncology & carcinogenesisBiophysicsSoybean ProteinsPeptidesOxidation-ReductionFunction (biology)Peptides
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Can copper(II) mediate Hoogsteen base-pairing in a left-handed DNA duplex? A pulse EPR study

2010

Pulse EPR spectroscopy is sued to investigate possible structural features of the copper(II) ion coordinated to poly(dG-dC) poly(dG-dC) in a frozen aqueous solution, and the structural change of the polynucleotide induced by the presence of the metal ion. Two different copper species were identified and their geometry explained by a molecular model. According to this model, one species is exclusively coordinated to a single guanine with the N7 nitrogen atom forming a coordinative bond with the copper. In the other species, a guanine and a cytosine form a ternary complex together with the copper ion. A copper crosslink between the N7 of guanine and N3 of cytosine is proposed as the most prob…

10120 Department of ChemistryCircular dichroismGuanineStereochemistryHoogsteen base pairrame strutture del DNA basi nucleotidiche EPR a impulsi risonanza paramagneticachemistry.chemical_elementTriple-stranded DNA3107 Atomic and Molecular Physics and OpticsNucleobasechemistry.chemical_compoundPolydeoxyribonucleotidesDNA structures540 ChemistryDNA Z-FormPhysical and Theoretical ChemistryBase PairingTernary complexCircular Dichroismstructure elucidationElectron Spin Resonance Spectroscopypulse EPIR spectroscopynucleobasesCopperSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Atomic and Molecular Physics and Opticschemistrycopper1606 Physical and Theoretical ChemistryCytosine
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Magnetic dichroism in angle-resolved hard x-ray photoemission from buried layers

2011

This work reports the measurement of magnetic dichroism in angular-resolved photoemission from in-plane magnetized buried thin films. The high bulk sensitivity of hard x-ray photoelectron spectroscopy (HAXPES) in combination with circularly polarized radiation enables the investigation of the magnetic properties of buried layers. HAXPES experiments with an excitation energy of 8 keV were performed on exchange-biased magnetic layers covered by thin oxide films. Two types of structures were investigated with the IrMn exchange-biasing layer either above or below the ferromagnetic layer: one with a CoFe layer on top and another with a Co${}_{2}$FeAl layer buried beneath the IrMn layer. A pronou…

420Materials scienceMagnetic momentCondensed matter physicsAnalytical chemistryDichroismengineering.materialCondensed Matter PhysicsHeusler compoundElectronic Optical and Magnetic Materialscircularly polarized x-raysCondensed Matter::Materials ScienceX-ray photoelectron spectroscopyFerromagnetismX-ray magnetic circular dichroismmagnetic dichroismangular-resolved hard x-ray photoemissionengineeringThin filmExcitationPhysical Review B
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Thermal induced conformational changes involved in the aggregation of beta-lactoglobulin

2005

Aggregation of proteins appears to be associated most often with conformational and structural changes that lead to exposure of some apolar residues. Depending on the native structure of the protein in exam, aggregation is a process that involves different mechanisms, whose time of occurrence and interplay can depend upon temperature. To single out information about the multistages of the aggregation pathway, here we investigate the thermally induced conformational and structural changes of the beta-lactoglobulin (BLG). The experimental approach consists in studying steady-state fluorescence spectra of intrinsic chromophores, two tryptophans, and Anylino-Naphthalene-Sulfonate dye (ANS) mole…

ANS emissionBeta-lactoglobulinProtein aggregationRayleigh scatteringCircular dichroismConformational changeFluorescence
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