Search results for "thioflavin T"

showing 10 items of 23 documents

Nouvelles perspectives concernant la structure et la fonction du domaine carboxyl terminal de Hfq

2015

Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA). The Escherichia coli Hfq is structurally organized into two domains. An N-terminal domain that folds as strongly bent β-sheets within individual protomers to…

IDP intrinsically-disordered proteinslcsh:Lifelcsh:QR1-502sub-membrane macromolecular assemblyPlasma protein bindingsRNA small non-coding RNABiochemistrylcsh:Microbiologyamyloid fibrilsProtein biosynthesis0303 health sciences[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]Escherichia coli Proteins030302 biochemistry & molecular biologyHfqCTRp Hfq C-terminal peptideFTIR Fourier transform infrared spectroscopyNTR N-terminal regionCompartmentalization (psychology)Cell biology[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsRNA Bacterialsmall non-coding ribonucleic acid (RNA)BiochemistryFSD Fourier self-deconvolutionTransfer RNAAmyloid fibrilProtein BindingBiophysicsBiologyHost Factor 1 Protein03 medical and health sciencesEscherichia coliThT thioflavin T[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyProtein Structure QuaternaryncRNA regulatory non-coding RNAPost-transcriptional regulationMolecular Biology030304 developmental biologyOriginal PaperC-terminusRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyCell Biologycellular compartmentalizationWT wild-typeProtein Structure Tertiarylcsh:QH501-531Host Factor 1 ProteinCTR Hfq C-terminal regionribonucleic acid (RNA) processing and degradationBiophysicpost-transcriptional regulationBioscience Reports
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Self-Organization Pathways and Spatial Heterogeneity in Insulin Amyloid Fibril Formation

2009

At high temperature and low pH, the protein hormone insulin is highly prone to form amyloid fibrils, and for this reason it is widely used as a model system to study fibril formation mechanisms. In this work, we focused on insulin aggregation mechanisms occurring in HCl solutions (pH 1.6) at 60 degrees C. By means of in situ Thioflavin T (ThT) staining, the kinetics profiles were characterized as a function of the protein concentration, and two concurrent aggregation pathways were pointed out, being concentration dependent. In correspondence to these pathways, different morphologies of self-assembled protein molecules were detected by atomic force microscopy images also evidencing the prese…

In situAmyloidHot Temperaturemedicine.medical_treatmentKineticsNucleationMicroscopy Atomic ForceFibrilchemistry.chemical_compoundMicroscopyMaterials ChemistrymedicineAnimalsInsulinBenzothiazolesPhysical and Theoretical ChemistryInsulin Amyloid Fibrils Secondary Nucleation Thioflavin T (ThT) Scanning Force Microscopy (SFM) Spatial HeterogeneityChemistryInsulinfluorescence spectroscopyFluorescenceSurfaces Coatings and FilmsThiazolesBiochemistryBiophysicsCattleThioflavinHydrochloric AcidProtein aggregation
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Conformational Transitions upon Maturation Rule Surface and pH-Responsiveness of α-Lactalbumin Microparticulates

2021

De novo designed protein supramolecular structures are nowadays attracting much interest as highly performing biomaterials. While a clear advantage is provided by the intrinsic biocompatibility and...

LactalbuminAmyloidFluorescence-lifetime imaging microscopyAmyloidBiocompatibilitySurface PropertiesChemistryBiochemistry (medical)Biomedical EngineeringSupramolecular chemistryBiocompatible MaterialspH-responsivenessGeneral ChemistryMicroparticlesHydrogen-Ion ConcentrationFluorescence Lifetime ImagingBiomaterialsMaturationMaterials TestingThioflavin TLactalbuminBiophysicsProtein CondensatesParticle SizeLiquid-Liquid Phase SeparationACS Applied Bio Materials
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Designing trehalose-conjugated peptides for the inhibition of Alzheimer’s Aβ oligomerization and neurotoxicity

2008

Neurotoxicity Alzheimer Amyloidsbeta-sheet breaker peptides • amyloid-beta • trehalose • SFM • neuronal cultures • thioflavin T
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Thioflavin T templates amyloid β(1–40) conformation and aggregation pathway

2015

Aβ(1-40) peptide supramolecular assembly and fibril formation processes are widely recognized to have direct implications in the progression of Alzheimer's disease. The molecular basis of this biological process is still unknown and there is a strong need of developing effective strategies to control the occurring events. To this purpose the exploitation of small molecules interacting with Aβ aggregation represents one of the possible routes. Moreover, the use specific labeling has represented so far one of the most common and effective methods to investigate such a process. This possibility in turn rests on the reliability of the probe/labels involved. Here we present evidences of the effe…

Protein StructureSecondaryAβ(1–40) peptideAmyloidProtein ConformationMolecular Sequence DataBiophysicsSupramolecular chemistryMolecular Dynamics SimulationProtein aggregationProtein Aggregation PathologicalBiochemistryProtein Structure SecondarySupramolecular assemblyProtein Aggregateschemistry.chemical_compoundProtein structureAlzheimer DiseasePathologicalSecondary structureAβ(1-40) peptideHumansBenzothiazolesAmino Acid SequenceFluorescent DyesAmyloid beta-PeptidesProtein StabilityOrganic ChemistryAlzheimer's diseaseProtein AggregationSmall moleculePeptide FragmentsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Peptide ConformationAlzheimer's disease; Aβ(1–40) peptide; Protein aggregation; Protein conformation; Secondary structure; Thioflavin T; Alzheimer Disease; Amino Acid Sequence; Amyloid beta-Peptides; Fluorescence Recovery After Photobleaching; Fluorescent Dyes; Humans; Molecular Dynamics Simulation; Molecular Sequence Data; Peptide Fragments; Protein Aggregates; Protein Aggregation Pathological; Protein Conformation; Protein Multimerization; Protein Stability; Protein Structure Secondary; ThiazolesThiazolesBiophysicBiochemistrychemistryThioflavin TBiophysicsThioflavinProtein MultimerizationFluorescence Recovery After PhotobleachingBiophysical Chemistry
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Carnosine inhibits amyloid fibril formation of alpha crystallin under destabilizing conditions

2008

SFM Scanning Force MicroscopyCD Circular DichroismThT Thioflavin THEPES 4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acidDSC Differential Scanning Calorimetry
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Inhibition of α-crystallin amyloid fibrils formation by carnosine

2008

SFM Scanning Force MicroscopyCD Circular DichroismThT Thioflavin THEPES 4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acidDSC Differential Scanning Calorimetry
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Effect of the heat treatment on α-crystallin : characterisation of amyloid fibrils formation and inhibitory effect of carnosine

2009

SFM Scanning Force MicroscopyCD Circular DichroismThT Thioflavin THEPES 4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acidDSC Differential Scanning Calorimetry
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High Fluorescence of Thioflavin T Confined in Mesoporous Silica Xerogels

2013

Trapping of organic molecules and dyes within nanoporous matrices is of great interest for the potential creation of new materials with tailored features and, thus, different possible applications ranging from nanomedicine to material science. The understanding of the physical basis of entrapment and the spectral properties of the guest molecules within the host matrix is an essential prerequisite for the design and control of the properties of these materials. In this work, we show that a mesoporous silica xerogel can efficiently trap the dye thioflavin T (ThT, a molecule used as a marker of amyloid fibrils and with potential drug benefits), sequestering it from an aqueous solution and pro…

Silicon dioxideSurface PropertiesSurface PropertieQuantum yieldNanotechnologyCondensed Matter PhysicPhotochemistryThioflavin T Fluorescence XerogelMesoporous materialFluorescencechemistry.chemical_compoundElectrochemistryMoleculeGeneral Materials ScienceBenzothiazolesParticle SizeSpectroscopyGelMolecular StructureChemistryNanoporousSurfaces and InterfacesMesoporous silicaCondensed Matter PhysicsSilicon DioxideFluorescenceSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)ThiazolesSpectrometry FluorescenceNanomedicineThioflavinMaterials Science (all)ThiazoleSurfaces and InterfaceGelsPorosity
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Biochar from Wood Chips and Corn Cobs for Adsorption of Thioflavin T and Erythrosine B.

2022

Biochars from wood chips (WC) and corn cobs (CC) were prepared by slow pyrolysis and used for sorption separation of erythrosine B (EB) and thioflavin T (TT) in batch experiments. Biochar-based adsorbents were extensively characterized using FTIR, XRD, SEM-EDX, and XPS techniques. The kinetics studies revealed that adsorption on external surfaces was the rate-limiting step for the removal of TT on both WC and CC biochar, while intraparticle diffusion was the rate-limiting step for the adsorption of EB. Maximal experimental adsorption capacities Qmaxexp of TT reached 182 ± 5 (WC) and 45 ± 2 mg g−1 (CC), and EB 12.7 ± 0.9 (WC) and 1.5 ± 0.4 mg g−1 (CC),…

adsorption kineticthioflavin Tisothermwood chipseryhrosine Bcorn cobbiocharGeneral Materials Sciencewood chips; corn cobs; biochar; thioflavin T; eryhrosine B; adsorption kinetics; isothermMaterials (Basel, Switzerland)
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