Search results for " Atomic"

showing 10 items of 1098 documents

Microtubule disruption changes endothelial cell mechanics and adhesion

2019

AbstractThe interest in studying the mechanical and adhesive properties of cells has increased in recent years. The cytoskeleton is known to play a key role in cell mechanics. However, the role of the microtubules in shaping cell mechanics is not yet well understood. We have employed Atomic Force Microscopy (AFM) together with confocal fluorescence microscopy to determine the role of microtubules in cytomechanics of Human Umbilical Vein Endothelial Cells (HUVECs). Additionally, the time variation of the adhesion between tip and cell surface was studied. The disruption of microtubules by exposing the cells to two colchicine concentrations was monitored as a function of time. Already, after 3…

0301 basic medicineCell biologyIntravital MicroscopyScienceConfocalCellBiophysicsCell Culture Techniques02 engineering and technologyMicroscopy Atomic ForceMechanotransduction CellularMicrotubulesArticleUmbilical veinCell Line03 medical and health sciencesMicrotubuleCell AdhesionHuman Umbilical Vein Endothelial CellsFluorescence microscopemedicineHumansCytoskeletonCytoskeletonMicroscopy ConfocalMultidisciplinaryDose-Response Relationship DrugChemistryPhysicsQRMechanicsAdhesion021001 nanoscience & nanotechnologyMaterials scienceApplied physicsEndothelial stem cell030104 developmental biologymedicine.anatomical_structureMicroscopy FluorescenceMedicineBiomaterials - cellsColchicine0210 nano-technologyBiological physicsScientific Reports
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Resveratrol-Induced Temporal Variation in the Mechanical Properties of MCF-7 Breast Cancer Cells Investigated by Atomic Force Microscopy

2019

Atomic force microscopy (AFM) combined with fluorescence microscopy has been used to quantify cytomechanical modifications induced by resveratrol (at a fixed concentration of 50 &micro

0301 basic medicineCellMotilityBreast Neoplasmsforce spectroscopyResveratrolresveratrolMicroscopy Atomic Forcefluorescence microscopyCatalysisArticleInorganic Chemistrylcsh:Chemistry03 medical and health scienceschemistry.chemical_compound0302 clinical medicinebreast cancerCell MovementElastic ModulusmedicineFluorescence microscopeCell AdhesionHumansPhysical and Theoretical ChemistryMolecular Biologylcsh:QH301-705.5SpectroscopyMechanical Phenomenaatomic force microscopyChemistryOrganic ChemistryForce spectroscopytechnology industry and agricultureGeneral MedicineAdhesioncytomechanicsComputer Science Applications030104 developmental biologymedicine.anatomical_structureMCF-7lcsh:Biology (General)lcsh:QD1-999030220 oncology & carcinogenesisCancer cellBiophysicsMCF-7 CellsFemaleMCF-7International Journal of Molecular Sciences
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Ethanol Controls the Self-Assembly and Mesoscopic Properties of Human Insulin Amyloid Spherulites.

2018

Protein self-assembly into amyloid fibrils or highly hierarchical superstructures is closely linked to neurodegenerative pathologies as Alzheimer's and Parkinson's diseases. Moreover, protein assemblies also emerged as building blocks for bioinspired nanostructured materials. In both the above mentioned fields, the main challenge is to control the growth and properties of the final protein structure. This relies on a more fundamental understanding of how interactions between proteins can determine structures and functions of biomolecular aggregates. Here, we identify a striking effect of the hydration of the single human insulin molecule and solvent properties in controlling hydrophobicity/…

0301 basic medicineCircular dichroismAmyloidAmyloidInsulins02 engineering and technologyMicroscopy Atomic Force03 medical and health scienceschemistry.chemical_compoundProtein structureMicroscopy Electron TransmissionScattering Small AngleSpectroscopy Fourier Transform InfraredMaterials ChemistryMoleculeHumansPhysical and Theoretical ChemistryAMYLOID SPECTROSOPY FLUORECENCE MICROSCOPYMesoscopic physicsEthanolMicroscopy ConfocalEthanolChemistryCircular DichroismOptical Imaging021001 nanoscience & nanotechnologySurfaces Coatings and FilmsNeutron Diffraction030104 developmental biologySpheruliteBiophysics0210 nano-technologySuperstructure (condensed matter)Hydrophobic and Hydrophilic Interactions
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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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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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Three-dimensional multiple-particle tracking with nanometric precision over tunable axial ranges

2017

The precise localization of nanometric objects in three dimensions is essential to identify functional diffusion mechanisms in complex systems at the cellular or molecular level. However, most optical methods can achieve high temporal resolution and high localization precision only in two dimensions or over a limited axial (z) range. Here we develop a novel wide-field detection system based on an electrically tunable lens that can track multiple individual nanoscale emitters in three dimensions over a tunable axial range with nanometric localization precision. The optical principle of the technique is based on the simultaneous acquisition of two images with an extended depth of field while …

0301 basic medicineOptical devicesMaterials scienceComplex system02 engineering and technologyTracking (particle physics)Deformable mirrorlaw.invention03 medical and health sciencesOpticsPosition (vector)lawAtomic and Molecular PhysicsElectronicImaging systemsDepth of fieldOptical and Magnetic MaterialsFluorescence microscopy; Imaging systems; Microscopy; Optical devices; Three-dimensional image processing; Electronic; Optical and Magnetic Materials; Atomic and Molecular Physics; and OpticsFluorescence microscopyMicroscopybusiness.industryThree-dimensional image processingFluorescence microscopy; Imaging systems; Microscopy; Optical devices; Three-dimensional image processing; Electronic Optical and Magnetic Materials; Atomic and Molecular Physics and Optics021001 nanoscience & nanotechnologyAtomic and Molecular Physics and OpticsElectronic Optical and Magnetic MaterialsNumerical apertureLens (optics)030104 developmental biologyTemporal resolutionand Optics0210 nano-technologybusinessFluorescence microscopy Imaging systems Microscopy Optical devices Three-dimensional image processing Electronic Optical and Magnetic Materials Atomic and Molecular Physics and Optics
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Nuclear inclusions of pathogenic ataxin-1 induce oxidative stress and perturb the protein synthesis machinery

2020

Spinocerebellar ataxia type-1 (SCA1) is caused by an abnormally expanded polyglutamine (polyQ) tract in ataxin-1. These expansions are responsible for protein misfolding and self-assembly into intranuclear inclusion bodies (IIBs) that are somehow linked to neuronal death. However, owing to lack of a suitable cellular model, the downstream consequences of IIB formation are yet to be resolved. Here, we describe a nuclear protein aggregation model of pathogenic human ataxin-1 and characterize IIB effects. Using an inducible Sleeping Beauty transposon system, we overexpressed the ATXN1(Q82) gene in human mesenchymal stem cells that are resistant to the early cytotoxic effects caused by the expr…

0301 basic medicineSCA1 Spinocerebellar ataxia type-1Intranuclear Inclusion BodiesClinical BiochemistryMSC mesenchymal stem cellProtein aggregationBiochemistry0302 clinical medicineMutant proteinProtein biosynthesisDE differentially expressed genesNuclear proteinlcsh:QH301-705.5FTIR Fourier-transform infrared spectroscopyAtaxin-1lcsh:R5-920biologyChemistryNuclear ProteinspolyQ polyglutamineRibosomeCell biologySB Sleeping BeautyRibosome ; Polyglutamine ; Ataxin-1 ; Oxidative stress ; Transposon ; Sleeping beauty transposon ; Protein networkSpinocerebellar ataxiaProtein foldingCellular modelFunction and Dysfunction of the Nervous Systemlcsh:Medicine (General)Research PaperiPSC induced pluripotent stem cellAtaxin 1Nerve Tissue ProteinsPPI protein-protein interaction03 medical and health sciencesROS reactive oxygen speciesProtein networkSleeping beauty transposonGSEA Gene Set Enrichment AnalysismedicineHumansNPC neural progenitor cellOrganic Chemistrymedicine.diseaseAFM atomic force microscopyOxidative Stress030104 developmental biologylcsh:Biology (General)IIBs intranuclear inclusion bodiesMS mass spectrometryCardiovascular and Metabolic Diseasesbiology.proteinPolyglutamine030217 neurology & neurosurgery
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Mechanisms of astringency: Structural alteration of the oral mucosal pellicle by dietary tannins and protective effect of bPRPs

2018

International audience; The interaction of tannins with salivary proteins is involved in astringency. This paper focussed on saliva liningoral mucosae, the mucosal pellicle. Using a cell-based model, the impact of two dietary tannins (EgC and EgCG)on the mucosal pellicle structure and properties was investigated by microscopic techniques. The role of basicProline-Rich-Proteins (bPRPs) in protecting the mucosal pellicle was also evaluated.At low (0.05 mM) tannin concentration, below the sensory detection threshold, the distribution of salivarymucins MUC5B on cells remained unaffected. At 0.5 and 1 mM, MUC5B-tannin aggregates were observed andtheir size increased with tannin concentration and…

0301 basic medicineSalivaFrictionAstringencyMicroscopy Atomic ForceCatechinCell LineAnalytical ChemistryProtein Aggregates03 medical and health sciences0404 agricultural biotechnologyHumansTanninDental PellicleFood scienceSalivaAstringentsEgCGchemistry.chemical_classificationR146/MUC1 cells030109 nutrition & dietetics[PHYS.PHYS]Physics [physics]/Physics [physics]ChemistryAtomic force microscopyDetection thresholdSalivary mucins MUC5BMucinMouth Mucosa04 agricultural and veterinary sciencesGeneral MedicineMucin-5B040401 food scienceDietSalivary Proline-Rich ProteinsAtomic Force MicroscopyOn cellsMicroscopy Electron ScanningSalivary ProteinsIB5Scanning Electron MicroscopyTannins[SDV.AEN]Life Sciences [q-bio]/Food and NutritionFood Science
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Heat- and pH-induced BSA conformational changes, hydrogel formation and application as 3D cell scaffold

2016

Aggregation and gelation of globular proteins can be an advantage to generate new forms of nanoscale biomaterials based on the fibrillar architecture. Here, we report results obtained by exploiting the proteins' natural tendency to self-organize in 3D network, for the production of new material based on BSA for medical application. In particular, at five different pH values the conformational and structural changes of the BSA during all the steps of the thermal aggregation and gelation have been analyzed by FTIR spectroscopy. The macroscopic mechanical properties of these hydrogels have been obtained by rheological measurements. The microscopic structure of the gels have been studied by AFM…

0301 basic medicineScaffoldHot TemperatureNanostructureBSACell SurvivalProtein ConformationGlobular proteinBiophysics?-aggregatesBiocompatible Materials02 engineering and technologymacromolecular substancesMicroscopy Atomic ForceBiochemistryMice03 medical and health sciencesProtein structureRheologySpectroscopy Fourier Transform Infraredβ-aggregateAnimalsCell-scaffoldFourier transform infrared spectroscopyMolecular BiologyNanoscopic scalechemistry.chemical_classificationTissue ScaffoldsChemistrySerum Albumin BovineHydrogelsHydrogen-Ion Concentration021001 nanoscience & nanotechnologySettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)NanostructuresHydrogelCrystallography030104 developmental biologyMechanical spectraBiophysicChemical engineeringFTIRSelf-healing hydrogelsMicroscopy Electron ScanningCattleStress MechanicalRheology0210 nano-technology
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Fast Inertia-Free Volumetric Light-Sheet Microscope

2017

Fast noninvasive three-dimensional (3D) imag-ing is crucial for quantitatively studying highly dynamic events ranging from flow cytometry to developmental biology. Light-sheet microscopy has emerged as the tool-of-choice for 3D characterization of rapidly evolving systems. However, to obtain a 3D image, either the sample or parts of the microscope are moved, limiting the acquisition speed. Here, we propose a novel inertia-free light-sheet-based scheme for volumetric imaging at high temporal resolution. Our approach comprises a novel combination of an acousto-optic scanner to produce tailored illumination and an acoustic-optofluidic lens, placed in the detection path to provide extended dept…

0301 basic medicineScanneracouto-optic devicesMaterials scienceMicroscopethree-dimensional microscopy01 natural sciencesAcouto-optic devices flow cytometry light-sheet microscopy three-dimensional microscopy Electronic Optical and Magnetic Materials Biotechnology Atomic and Molecular Physics and Optics Electrical and Electronic Engineeringlaw.invention010309 optics03 medical and health sciencesOpticslawAtomic and Molecular Physics0103 physical sciencesMicroscopyElectronicOptical and Magnetic MaterialsElectrical and Electronic Engineeringbusiness.industryflow cytometryRangingFrame rateAtomic and Molecular Physics and OpticsElectronic Optical and Magnetic MaterialsCharacterization (materials science)Lens (optics)acouto-optic devices; flow cytometry; light-sheet microscopy; three-dimensional microscopy; Electronic Optical and Magnetic Materials; Biotechnology; Atomic and Molecular Physics and Optics; Electrical and Electronic Engineering030104 developmental biologyLight sheet fluorescence microscopyand Opticsbusinesslight-sheet microscopyBiotechnologyACS Photonics
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