Search results for " Scanning Force Microscopy"

showing 6 items of 6 documents

Protective Effects of L- and D-Carnosine on R-Crystallin Amyloid Fibril Formation: Implications for Cataract Disease

2009

Mildly denaturing conditions induce bovine ?-crystallin, the major structural lens protein, to self-assemble into fibrillar structures in vitro. The natural dipeptide L-carnosine has been shown to have potential protective and therapeutic significance in many diseases. Carnosine derivatives have been proposed as potent agents for ophthalmic therapies of senile cataracts and diabetic ocular complications. Here we report the inhibitory effect induced by the peptide (L- and D-enantiomeric form) on ?-crystallin fibrillation and the almost complete restoration of the chaperone activity lost after denaturant and/or heat stress. Scanning force microscopy (SFM), thioflavin T, and a turbidimetry ass…

CrystallinCircular dichroismAmyloidCarnosinePeptideMicroscopy Atomic ForceBiochemistryCataractLens proteinRats Sprague-Dawleychemistry.chemical_compoundOrgan Culture TechniquesCrystallinChaperone activityAnimalsalpha-CrystallinsSFM Scanning Force Microscopychemistry.chemical_classificationDipeptideCD Circular DichroismThT Thioflavin TCalorimetry Differential ScanningDSC Differential Scanning CalorimetryCircular DichroismCarnosineStereoisomerismIn vitroeye diseasesRatsSpectrometry FluorescencechemistryBiochemistryHEPES 4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acidThioflavinCattleFemaleSpectrophotometry Ultravioletsense organsAmyloid fibrilMolecular Chaperones
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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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Assembly of modular asymmetric organic-inorganic polyoxometalate hybrids into anisotropic nanostructures.

2010

Three organic-inorganic hybrid Mn-Anderson polyoxometalates (POMs), with both symmetrical and asymmetrical appended groups, have been synthesized, identified using electrospray mass spectrometry, and isolated using an approach that allows the three AA, BB, and AB compounds to be structurally characterized. Investigation of the self-assembly of the hybrids on hydrophilic surfaces reveals the formation of nanofibres with characteristics that reflect the nature of the substitution of the POM yielding a route to the programmed assembly of anisotropic hybrid nanostructures.

Models MolecularNanostructureElectrospray mass spectrometryChemistryGeneral ChemistryTungsten CompoundsBiochemistryCatalysisMass SpectrometryNanostructuresSelf-assembly Langmuir-Blodgett Scanning Force Microscopy Polyoxomethalates Hybrid Anysotropic NanostructuresColloid and Surface ChemistryChemical engineeringInorganic ChemicalsPolyoxometalateOrganic inorganicOrganic chemistryAnisotropyOrganic ChemicalsAnisotropySettore CHIM/02 - Chimica FisicaHybridJournal of the American Chemical Society
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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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