Search results for "SPHERULITES"

showing 4 items of 4 documents

The Use of Wild Plants in the Palaeolithic and Neolithic of Northwestern Africa: Preliminary Results from the PALEOPLANT Project

2018

Carrión Marco Y., Morales J., Portillo M., Pérez-Jordà G., Peña-Chocarro L., Zapata L. (2018) The Use of Wild Plants in the Palaeolithic and Neolithic of Northwestern Africa: Preliminary Results from the PALEOPLANT Project. En: Mercuri A., D'Andrea A., Fornaciari R., Höhn A. (eds.) Plants and People in the African Past. Springer, Cham

0301 basic medicine010506 paleontologyPleistocenePhytolithsved/biology.organism_classification_rank.species01 natural sciencesSpherulites03 medical and health sciencesChamaeropsGlacial periodNeolithicCharcoalHolocene0105 earth and related environmental sciencesStipa tenacissimaPalaeolithicFood plantsbiologyEcologyved/biologyVegetation15. Life on landbiology.organism_classification030104 developmental biologyGeographyvisual_artCharcoalSeedsvisual_art.visual_art_mediumCalcitic microfossilsNorthwestern AfricaJuniperBasketry
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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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Probing ensemble polymorphism and single aggregate structural heterogeneity in insulin amyloid self-assembly.

2020

Ensembles of protein aggregates are characterized by a nano- and micro-scale heterogeneity of the species. This diversity translates into a variety of effects that protein aggregates may have in biological systems, both in connection to neurodegenerative diseases and immunogenic risk of protein drug products. Moreover, this naturally occurring variety offers unique opportunities in the field of protein-based biomaterials. In the above-mentioned fields, the isolation and structural analysis of the different amyloid types within the same ensemble remain a priority, still representing a significant experimental challenge. Here we address such complexity in the case of insulin for its relevance…

Fluorescence-lifetime imaging microscopyAmyloidFIBRIL POLYMORPHISMPHASOR APPROACHSURFACESpheruliteProtein ConformationSurface Propertiesmedicine.medical_treatmentBETATHIOFLAVIN-T FLUORESCENCE02 engineering and technologyMicro-FTIRProtein aggregation010402 general chemistryFibril01 natural sciencesFluorescence lifetime imagingBiomaterialsProtein AggregatesColloid and Surface ChemistryBINDINGHuman insulinmedicineInsulinParticle SizeSECONDARY STRUCTURESPHERULITESChemistryInsulinAmyloidosisOptical ImagingMICROSCOPY021001 nanoscience & nanotechnologymedicine.disease0104 chemical sciencesSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsBiopharmaceuticalMicroscopy FluorescenceAmyloid structureVisible and subvisible particlesBiophysicsThioflavin TSelf-assemblyHeterogeneity0210 nano-technologyInfrared microscopyPROTEIN AGGREGATIONJournal of colloid and interface science
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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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