Search results for "Aggregation"

showing 10 items of 566 documents

Oxidation effects in antiaggregogenic properties of Epigallocatechingallate

2021

Epigallocatechin-gallate (EGCG), the most abundant flavonoid in green tea, has been extensively studied for its potential in the treatment of amyloid related disorders. This molecule was found to modulate abnormal protein self-assembly, reducing resulting cellular toxicity. EGCG is known to suppress or to slow down the aggregation processes of several proteins, thus supporting the idea that general mechanisms regulate its anti-aggregogenic effects and, interestingly, in the oxidised form it demonstrated an higher efficiency in reducing protein aggregation with respect to intact molecule. We here investigate the effects of intact and oxidized EGCG the thermal aggregation pathway of Bovine Se…

Protein aggregation electrostatics EGCG-Protein interaction EGCG Oxidation.
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Aggregation processes of intrinsically disordered proteins: influence of the environment

Protein aggregation neurodegenerative diseases intrinsically disordered proteins beta amyloid peptide alpha-synucleinSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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Two distinct phases characterize thermal aggregation of b-Lactoglobulin at neutral pH

2011

Protein aggregationAFMConformational changeSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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Insights into amyloid fibrils dynamics from neutron scattering

2011

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Protein dynamics Aggregation concanavalin A
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Neutron Scattering Reveals Enhanced Protein Dynamics in Concanavalin A Amyloid Fibrils

2012

Protein aggregation is one of the most challenging topics in life sciences, and it is implicated in several human pathologies. The nature and the role of toxic species is highly debated, with amyloid fibrils being among the most relevant species for their peculiar structural and functional properties. Protein dynamics and in particular the ability to fluctuate through a large number of conformational substates are closely related to protein function. This Letter focuses on amyloid fibril dynamics, and, to our knowledge, it is the first neutron scattering study on a protein (Concanavalin A) isolated in its fibril state. Our results reveal enhanced atomic fluctuations in amyloid fibrils and i…

Protein functionbiologyChemistryProtein dynamicsmean square displacementsA proteinatomic fluctuationsmacromolecular substancesProtein aggregationNeutron scatteringFibrilAmyloid fibrilatomic fluctuationprotein aggregationCrystallographyConcanavalin ABiophysicsbiology.proteinGeneral Materials SciencePhysical and Theoretical Chemistry
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Purification and partial characterization of a lectin protein complex, the clathrilectin, from the calcareous sponge Clathrina clathrus

2016

Carbohydrate-binding proteins were purified from the marine calcareous sponge Clathrina clathrus via affinity chromatography on lactose and N-acetyl glucosamine- agarose resins. Proteomic analysis of acrylamide gel separated protein subunits obtained in reducing conditions pointed out several candidates for lectins. Based on amino- acid sequence similarity, two peptides displayed homology with the jack bean lectin Concanavalin A, 
 including a conserved domain shared by proteins in the L-type lectin superfamily. An N-acetyl glucosamine - binding protein complex, named clathrilectin, was further purified via gel filtration chromatography, bioguided with a diagnostic rabbit erythrocyte haemag…

Proteomics0301 basic medicinePhysiologySyconBiochemistry03 medical and health sciencesAffinity chromatographyLectinsAnimalsTrypsinMolecular Biology030102 biochemistry & molecular biologybiologyCalcareous spongeHemagglutinationLectinClathrina clathrusbiology.organism_classificationMolecular biologyCell aggregationPoriferaPorifera ; Clathrina clathrus ; lectin ; N-acetyl-glucosamine ; cell aggregation ; proteomicsSponge030104 developmental biologyBiochemistryConcanavalin AProteolysisbiology.proteinCarbohydrate MetabolismFemaleRabbitsComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
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Human apolipoprotein A-I natural variants: molecular mechanisms underlying amyloidogenic propensity

2012

Human apolipoprotein A-I (apoA-I)-derived amyloidosis can present with either wild-type (Wt) protein deposits in atherosclerotic plaques or as a hereditary form in which apoA-I variants deposit causing multiple organ failure. More than 15 single amino acid replacement amyloidogenic apoA-I variants have been described, but the molecular mechanisms involved in amyloid-associated pathology remain largely unknown. Here, we have investigated by fluorescence and biochemical approaches the stabilities and propensities to aggregate of two disease-associated apoA-I variants, apoA-IGly26Arg, associated with polyneuropathy and kidney dysfunction, and apoA-ILys107-0, implicated in amyloidosis in severe…

ProteomicsProtein Foldinglcsh:MedicineProtein aggregationpolymyxinsBiochemistryProtein Structure SecondaryMiceProtein structureneutrophilsMolecular Cell Biologypolycyclic compoundslcsh:ScienceCellular Stress ResponsesMultidisciplinaryProtein StabilityAmyloidosisCiencias QuímicasfluorescenseCell biologymacrophagesBiochemistryToxicityMedicineProtein foldinglipids (amino acids peptides and proteins)medicine.symptomPolyneuropathyResearch ArticleProtein StructureMedicinaLipoproteinsImmunologyBiophysicsInflammationAmyloidogenic ProteinsBiologyProtein ChemistryMicrobiologyCell Lineprotein aggregationmacrophage activationmedicineAnimalsHumansoligomersProtein InteractionsBiologyInflammationamyloidosisApolipoprotein A-IMacrophageslcsh:RImmunityProteinsnutritional and metabolic diseasesmedicine.diseaseApolipoproteinsAmino Acid SubstitutionCell cultureinflammationCiencias Médicaslcsh:QClinical ImmunologyMutant ProteinspolyneuropathyProtein Multimerization
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The role of metal ions in the thermal aggregation of Bovine Serum Albumin

2009

Raman scatteringBSAaggregationFTIR absortpion.metal ionSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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Actinopathies and Myosinopathies

2009

The currently recognized two forms of "anabolic" protein aggregate myopathies, that is, defects in development, maturation and final formation of respective actin and myosin filaments encompass actinopathies and myosinopathies. The former are marked by mutations in the ACTA1 gene, largely of the de novo type. Aggregates of actin filaments are deposited within muscle fibers. Early clinical onset is often congenital; most patients run a rapidly progressive course and die during their first 2 years of life. Myosinopathies or myosin storage myopathies also commence in childhood, but show a much more protracted course owing to mutations in the myosin heavy chain gene MYH7. Protein aggregation co…

Rapidly progressive courseGeneral Neurosciencemacromolecular substancesMyosinsProtein aggregationBiologyClinical onsetActinsPathology and Forensic MedicineCell biologyProtracted courseMuscular DiseasesBiochemistryMyosinHumansMYH7Neurology (clinical)MINI‐SYMPOSIUM: Protein Aggregate MyopathiesGeneActinBrain Pathology
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Kinetic evidence for the solubilization of pyridine-2-azo-p-dimethylaniline in alkanediyl-α,ω-bis(dimethylcetylammonium nitrate) surfactants. Role of…

2004

The incorporation of the bidentate ligand pyridine-2-azo-p-dimethylaniline (PADA) into micellar aggregates of the dimeric cationic surfactants propanediyl-, hexanediyl- and dodecanediyl-alpha,omega-bis(dimethylcetylammonium nitrate) (16-3-16,2NO(3)(-), 16-6-16,2NO(3)(-) and 16-12-16,2NO(3)(-), respectively) has been studied at 25 degreesC by examining the kinetics of the complexation reaction of the Ni(II) ion with this ligand. For comparison, cetyltrimethylammonium nitrate ( CTAN), which can be considered as the "monomeric'' surfactant of 16-3-16,2NO(3)(-), has also been used. The kinetic data have shown that, for 16-3-16,2NO(3)(-) and CTAN, at a surfactant concentration below the critical…

Reaction mechanismInorganic chemistryMicelleCATIONIC GEMINI SURFACTANTSCatalysisHydrophobic effectReaction rate constantPulmonary surfactantDIMERIC SURFACTANTSPolymer chemistryMaterials ChemistryWATERELECTRON TRANSFERANGLE NEUTRON SCATTERINGInterfaces (materials) Optical waveguides metal ionsAqueous solutionAGGREGATION PROPERTIESChemistryAQUEOUS SOLUTIONCationic polymerizationGeneral ChemistryANIONIC MICELLESSUBSTITUTED FERROCENESCritical micelle concentrationBROMIDE SURFACTANTSANGLE NEUTRON SCATTERING; CATIONIC GEMINI SURFACTANTS; AQUEOUS SOLUTION; BROMIDE SURFACTANTS; DIMERIC SURFACTANTS; SUBSTITUTED FERROCENES; AGGREGATION PROPERTIES; ELECTRON TRANSFER; ANIONIC MICELLES; WATERNew J. Chem.
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