Search results for " fluorescence lifetime"

showing 6 items of 6 documents

Polysorbate 80 controls Morphology, structure and stability of human insulin Amyloid-Like spherulites

2022

AbstractAmyloid protein aggregates are not only associated with neurodegenerative diseases and may also occur as unwanted by-products in protein-based therapeutics. Surfactants are often employed to stabilize protein formulations and reduce the risk of aggregation. However, surfactants alter protein-protein interactions and may thus modulate the physicochemical characteristics of any aggregates formed. Human insulin aggregation was induced at low pH in the presence of varying concentrations of the surfactant polysorbate 80. Various spectroscopic and imaging methods were used to study the aggregation kinetics, as well as structure and morphology of the formed aggregates. Molecular dynamics s…

Amyloid-like Spherulites Fluorescence Lifetime Imaging Aggregate Stability Polysorbate 80 Protein FormulationsAmyloidMorphology (linguistics)AmyloidChemistryInsulinmedicine.medical_treatmentIntermolecular forcePolysorbatesPolyvinyl alcoholSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsBiomaterialsSurface-Active Agentschemistry.chemical_compoundMolecular dynamicsColloid and Surface ChemistryPulmonary surfactantCritical micelle concentrationmedicineBiophysicsHumansInsulinMicelles
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Corrigendum to “Polysorbate 80 controls Morphology, structure and stability of human insulin Amyloid-Like spherulites” [J. Colloid Interface Sci. 606…

2023

Amyloid-like Spherulites Fluorescence Lifetime Imaging Aggregate Stability Polysorbate 80 Protein FormulationsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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Blue autofluorescence in protein aggregates “lighted on” by UV induced oxidation

2019

Oxidation of amino acid side chains in protein structure can be induced by UV irradiation leading to critical changes in molecular structure possibly modifying protein stability and bioactivity. Here we show, by using a combination of multiple spectroscopic techniques and Fluorescence Lifetime Imaging, that UV-light exposure induces irreversible oxidation processes in Ubiquitin structure. In particular, the growth of a new autofluorescence peak in the blue region is detected, that we attribute to tyrosine oxidation products. Blue autofluorescence intensity is found to progressively increase also during aggregation processes leading to the formation of aggregates of non-amyloid nature. Signi…

Dityrosine formation0301 basic medicineAmyloidUltraviolet RaysBiophysicsPeptideProtein aggregationAmyloid autofluorescence; Dityrosine formation; Fluorescence lifetime imaging; Oxidative stress; UbiquitinFluorescence lifetime imagingBiochemistryFluorescenceAnalytical ChemistryProtein Aggregates03 medical and health sciences0302 clinical medicineProtein structureHumansTyrosineMolecular Biologychemistry.chemical_classificationAmyloid beta-PeptidesUbiquitinChemistryFluorescenceAmino acidAutofluorescence030104 developmental biologyBiophysicsOxidative streAmyloid autofluorescenceOxidation-Reduction030217 neurology & neurosurgeryBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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Phasor-FLIM analysis of Thioflavin T self-quenching in Concanavalin amyloid fibrils

2020

The formation of amyloid structures has traditionally been related to human neurodegenerative pathologies and, in recent years, the interest in these highly stable nanostructures was extended to biomaterial sciences. A common method to monitor amyloid growth is the analysis of Thioflavin T fluorescence. The use of this highly selective dye, diffused worldwide, allows mechanistic studies of supramolecular assemblies also giving back important insight on the structure of these aggregates. Here we present experimental evidence of self-quenching effect of Thioflavin T in presence of amyloid fibrils. A significant reduction of fluorescence lifetime of this dye which is not related to the propert…

Fluorescence-lifetime imaging microscopyAmyloidFLIMHistologyAmyloid02 engineering and technologyProtein aggregationprotein aggregation03 medical and health scienceschemistry.chemical_compound0302 clinical medicineself-quenchingmental disordersamyloid fibrilConcanavalin Afluorescence lifetimeHumansBenzothiazolesInstrumentationFluorescent DyesInclusion BodiesQuenching (fluorescence)biologyStaining and LabelingChemistryOptical ImagingPhasorNeurodegenerative Diseases030206 dentistry021001 nanoscience & nanotechnologyFluorescenceSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Medical Laboratory TechnologyMicroscopy FluorescenceConcanavalin APhasorbiology.proteinBiophysicsThioflavin TThioflavinamyloid fibrils Concanavalin A FLIM fluorescence lifetime Phasor protein aggregation self-quenching Thioflavin TAnatomy0210 nano-technology
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Nile Red lifetime reveals microplastic identity

2020

Microplastic pollution is recognized as a worldwide environmental problem. The increasing daily use and release of plastics into the environment have led to the accumulation of fragmented microplastics, with potentially awful consequences for the environment, and animal and human health. The detection and identification of microplastics are of utmost importance, but available methods are still limited. In this work, a new approach is presented for the analysis of microplastics based on hydrophobic fluorescence staining with Nile Red, using spectrally resolved confocal fluorescence microscopy and fluorescence lifetime imaging microscopy (FLIM). Significant differences were observed in the em…

MicroplasticsFluorescence-lifetime imaging microscopyMicroplastics010501 environmental sciencesManagement Monitoring Policy and Law01 natural sciences03 medical and health sciencesHuman healthchemistry.chemical_compoundOxazinesFluorescence microscopeAnimalsHumansEnvironmental ChemistryFluorescence staining030304 developmental biology0105 earth and related environmental sciences0303 health sciencesChemistryPublic Health Environmental and Occupational HealthNile redGeneral MedicineFluorescenceSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)microplastics nile red fluorescence lifetime Environmental Monitoring Humans Microplastics Oxazines Plastics Water Pollutants ChemicalAquatic environmentBiological systemPlasticsWater Pollutants ChemicalEnvironmental MonitoringEnvironmental Science: Processes & Impacts
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Spectroscopic Properties of Holmium-Aluminum- Germanium Co-doped Silica Fiber

2020

We report the basic spectroscopic properties of a home-made holmium-aluminum-germanium co-doped silica fiber, designed for laser applications. We present the ground-state and excitedstate absorption spectra of the fiber along with the upconversion emission spectrum under laser action, which served for making an energy levels’ diagram of Ho3+ ion. We discuss the ways to assess the kinetics of Ho3+ 2-μm fluorescence, focusing on measuring fluorescence lifetime from 5I7 level and nonradiative decay time from 5I6 level. The simple analytical formulae, applicable for fitting of the fluorescence decay curve, are derived, which can be useful for precise modeling of holmiumdoped fiber lasers. PID20…

excited state absorptionup-conversion emission:FÍSICA [UNESCO]UNESCO::FÍSICAfluorescence lifetimePhysics::Opticsground-state absorptionholmium-doped silica fiberexcited state absorption; up-conversion emission; fluorescence lifetime
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