Search results for " Infrared"

showing 10 items of 945 documents

Molecular similarities and differences from human pulmonary fibrosis and corresponding mouse model: MALDI imaging mass spectrometry in comparative me…

2017

Animal models can reproduce some model-specific aspects of human diseases, but some animal models translate poorly or fail to translate to the corresponding human disease. Here, we develop a strategy to systematically compare human and mouse tissues, and conduct a proof-of-concept experiment to identify molecular similarities and differences using patients with idiopathic pulmonary fibrosis and a bleomycin-induced fibrosis mouse model. Our novel approach employs high-throughput tissue microarrays (TMAs) of humans and mice, high-resolution matrix-assisted laser desorption/ionization-Fourier transform-ion cyclotron resonance-mass spectrometry imaging (MALDI-FT-ICR-MSI) to spatially resolve ma…

0301 basic medicineMALDI imagingPulmonary FibrosisSecondary MetabolismComputational biologyBiologyBioinformaticsProof of Concept StudyPathology and Forensic MedicineBleomycinMice03 medical and health sciencesIdiopathic pulmonary fibrosisMetabolomicsSpecies SpecificityFibrosisAdministration InhalationSpectroscopy Fourier Transform InfraredPulmonary fibrosismedicineAnimalsCluster AnalysisHumansMetabolomicsLungPhysiology ComparativeMolecular BiologyAntibiotics AntineoplasticTissue microarrayCell BiologyCyclotronsmedicine.diseaseImmunohistochemistryDisease Models AnimalMatrix-assisted laser desorption/ionization030104 developmental biologyTissue Array AnalysisSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationImmunohistochemistryLaboratory Investigation
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Potential Second-Harmonic Ghost Bands in Fourier Transform Infrared (FT-IR) Difference Spectroscopy of Proteins

2018

Fourier transform infrared (FT-IR) difference absorption spectroscopy is a common method for studying the structural and dynamical aspects behind protein function. In particular, the 2800–1800 cm−1 spectral range has been used to obtain information about internal (deuterated) water molecules, as well as site-specific details about cysteine residues and chemically modified and artificial amino acids. Here, we report on the presence of ghost bands in cryogenic light-induced FT-IR difference spectra of the protein bacteriorhodopsin. The presence of these ghost bands can be particularly problematic in the 2800–1900 cm−1 region, showing intensities similar to O–D vibrations from water molecules…

0301 basic medicineMaterials scienceAbsorption spectroscopyInfraredAnalytical chemistryInfrared spectroscopy010402 general chemistry01 natural sciences03 medical and health sciencessymbols.namesakeSpectroscopy Fourier Transform InfraredFourier transform infrared spectroscopySpectroscopyInstrumentationSpectroscopybiologyProteinsBacteriorhodopsin0104 chemical sciences030104 developmental biologyApplied spectroscopyFourier transformBacteriorhodopsinssymbolsbiology.proteinArtifactsApplied Spectroscopy
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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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pH-sensitive vibrational probe reveals a cytoplasmic protonated cluster in bacteriorhodopsin

2017

Infrared spectroscopy has been used in the past to probe the dynamics of internal proton transfer reactions taking place during the functional mechanism of proteins but has remained mostly silent to protonation changes in the aqueous medium. Here, by selectively monitoring vibrational changes of buffer molecules with a temporal resolution of 6 µs, we have traced proton release and uptake events in the light-driven proton-pump bacteriorhodopsin and correlate these to other molecular processes within the protein. We demonstrate that two distinct chemical entities contribute to the temporal evolution and spectral shape of the continuum band, an unusually broad band extending from 2,300 to well…

0301 basic medicineModels MolecularCytoplasmNuclear TheoryMolecular ConformationInfrared spectroscopyIonic bondingProtonationBuffers010402 general chemistry53001 natural sciences03 medical and health sciencesDeprotonationSpectroscopy Fourier Transform InfraredMoleculeNuclear ExperimentMultidisciplinarybiologyChemistryWaterBacteriorhodopsinHydrogen-Ion Concentration0104 chemical sciencesKinetics030104 developmental biologyPNAS PlusChemical physicsCytoplasmTemporal resolutionBacteriorhodopsinsbiology.proteinPhysics::Accelerator PhysicsProtonsMetabolic Networks and PathwaysProtein Binding
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Back to the oligomeric state: pH-induced dissolution of concanavalin A amyloid-like fibrils into non-native oligomers

2016

The subtle interplay between long range electrostatic forces, hydrophobic interactions and short range protein-protein interactions regulates the onset/evolution of protein aggregation processes as well as the stability of protein supramolecular structures. Using a combination of FTIR spectroscopy, light scattering and advanced imaging, we present evidence on the main role of electrostatic forces in the formation and stability of amyloid-like fibrils formed from concanavalin A (ConA), a protein showing structural homology with the human serum amyloid protein. At high protein concentration, where protein-protein interactions cannot be neglected, we highlight a thermal-induced aggregation pat…

0301 basic medicineMorphology (linguistics)biologyChemistryGeneral Chemical EngineeringChemistry (all)Supramolecular chemistryGeneral ChemistryProtein aggregationFibrilHydrophobic effect03 medical and health sciencesCrystallography030104 developmental biologyConcanavalin Abiology.proteinChemical Engineering (all)Fourier transform infrared spectroscopyDissolutionRSC Advances
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Role of ATP during the initiation of microvascularization: acceleration of an autocrine sensing mechanism facilitating chemotaxis by inorganic polyph…

2018

The in vitro tube formation assay with human umbilical vein endothelial cells (HUVEC) was applied to identify the extra- and intracellular sources of metabolic energy/ATP required for cell migration during the initial stage of microvascularization. Extracellularly, the physiological energy-rich polymer, inorganic polyphosphate (polyP), applied as biomimetic amorphous calcium polyP microparticles (Ca-polyP-MP), is functioning as a substrate for ATP generation most likely via the combined action of the alkaline phosphatase (ALP) and the adenylate kinase (AK). The linear Ca-polyP-MP with a size of 40 phosphate units, close to the polyP in the acidocalcisomes in the blood platelets, were found …

0301 basic medicineOligomycinAdenylate kinaseNeovascularization PhysiologicBiochemistry03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAdenosine TriphosphateX-Ray DiffractionPolyphosphatesSpectroscopy Fourier Transform InfraredExtracellularHuman Umbilical Vein Endothelial CellsHumansGlycolysisMolecular BiologyTube formationATP synthasebiologyChemistryApyraseAdenylate Kinase (AK) ; Alkaline Phosphatase (ALP) ; ATP ; F0F1-ATP synthase ; inorganic polyphosphate ; microvascularization ; tube formation ; Human Umbilical Vein Endothelial Cells (HUVEC) ; nano/microparticles ; chemotaxis ; autocrine sensing.ChemotaxisCell BiologyCell biologyAutocrine Communication030104 developmental biology030220 oncology & carcinogenesisMicrovesselsbiology.proteinIntracellular
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Amorphous polyphosphate–hydroxyapatite: A morphogenetically active substrate for bone-related SaOS-2 cells in vitro

2015

There is increasing evidence that inorganic calcium-polyphosphates (polyP) are involved in human bone hydroxyapatite (HA) formation. Here we investigated the morphology of the particles, containing calcium phosphate (CaP) with different concentrations of various Na-polyP concentrations, as well as their effects in cell culture. We used both SaOS-2 cells and human mesenchymal stem cells. The polymeric phosphate readily binds calcium ions under formation of insoluble precipitates. We found that addition of low concentrations of polyP (10wt.%, referred to the CaP deposits) results in an increased size of the HA crystals. Surprisingly, at higher polyP concentrations (10wt.%) the formation of cr…

0301 basic medicinePolymersBiocompatible Materials02 engineering and technologyBone tissueBiochemistryApatitechemistry.chemical_compoundX-Ray DiffractionOsteogenesisPolyphosphatesSpectroscopy Fourier Transform InfraredTissue ScaffoldsBiomaterialGeneral Medicine021001 nanoscience & nanotechnologyMicrospheresGene Expression Regulation Neoplasticmedicine.anatomical_structureBiochemistryvisual_artvisual_art.visual_art_mediumAlkaline phosphataseHydroxyapatites0210 nano-technologyBiotechnologyMaterials scienceBiocompatibilityBiomedical Engineeringchemistry.chemical_elementCalciumCollagen Type IBiomaterials03 medical and health sciencesCalcification PhysiologicMicroscopy Electron TransmissionCell Line TumormedicineHumansBone regenerationMolecular BiologyCell ProliferationIonsOsteoblastsTissue EngineeringSodiumMesenchymal Stem CellsAlkaline PhosphatasePhosphateMicroscopy ElectronDurapatite030104 developmental biologychemistryBiophysicsCalciumActa Biomaterialia
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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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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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Pressure effects on α-synuclein amyloid fibrils: An experimental investigation on their dissociation and reversible nature

2017

α–synuclein amyloid fibrils are found in surviving neurons of Parkinson's disease affected patients, but the role they play in the disease development is still under debate. A growing number of evidences points to soluble oligomers as the major cytotoxic species, while insoluble fibrillar aggregates could even play a protection role. In this work, we investigate α–synuclein fibrils dissociation induced at high pressure by means of Small Angle X-ray Scattering and Fourier Transform Infrared Spectroscopy. Fibrils were produced from wild type α–synuclein and two familial mutants, A30P and A53T. Our results enlighten the different reversible nature of α–synuclein fibrils fragmentati…

0301 basic medicineSmall AngleAmyloidHigh-pressureMutantBiophysicsmacromolecular substances010402 general chemistryFibril01 natural sciencesBiochemistryDissociation (chemistry)Scattering03 medical and health scienceschemistry.chemical_compoundX-Ray DiffractionScattering Small AngleSpectroscopy Fourier Transform InfraredPressureHumansPoint MutationFourier transform infrared spectroscopyMolecular BiologySpectroscopyAlpha-synucleinAmyloid; FTIR; High-pressure; SAXS; α-synuclein; Amyloid; Humans; Parkinson Disease; Point Mutation; Pressure; Scattering Small Angle; Solubility; Spectroscopy Fourier Transform Infrared; X-Ray Diffraction; alpha-Synuclein; Biophysics; Biochemistry; Molecular BiologySmall-angle X-ray scatteringWild typeα-synucleinParkinson DiseaseSAXSAmyloid fibril0104 chemical sciences?-synucleinCrystallography030104 developmental biologyBiophysicchemistryFTIRSolubilityFourier Transform InfraredBiophysicsalpha-SynucleinHuman
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