Search results for "PEPTIDE"

showing 10 items of 4589 documents

Cholesterol binding to amyloid-β fibrils: A TEM study

2008

There is increasing interest in the role of brain cholesterol in Alzheimer's disease and the contribution of cholesterol to the formation of amyloid plaques. This paper presents a TEM study showing the binding of soluble approximately 10 nm diameter cholesterol-PEG 600 micelles to amyloid-beta(1-42) (Abeta(1-42)) fibrils formed either in the presence of this cholesterol derivative or to preformed fibrils generated under four different fibrillogenesis conditions. Specimens negatively stained with uranyl acetate revealed that during 24 h fibrillogenesis at 37 degrees C the cholesterol-PEG micelles bound periodically to Abeta(1-42) protofibrils and apparently also formed a thin smooth unbroken…

AmyloidAmyloid beta-PeptidesCholesterolCholesterol bindingGeneral Physics and AstronomyUranyl acetateFibrillogenesismacromolecular substancesCell BiologyFibrilNegative stainMicellePolyethylene GlycolsCrystallographychemistry.chemical_compoundCholesterolMicroscopy Electron TransmissionchemistryStructural BiologyHumanslipids (amino acids peptides and proteins)General Materials ScienceHydrogen peroxideMicellesMicron
researchProduct

Detection of Amyloid-β Fibrils Using Track-Etched Nanopores: Effect of Geometry and Crowding

2021

Several neurodegenerative diseases have been linked to proteins or peptides that are prone to aggregate in different brain regions. Aggregation of amyloid-β (Aβ) peptides is recognized as the main cause of Alzheimer's disease (AD) progression, leading to the formation of toxic Aβ oligomers and amyloid fibrils. The molecular mechanism of Aβ aggregation is complex and still not fully understood. Nanopore technology provides a new way to obtain kinetic and morphological aspects of Aβ aggregation at a single-molecule scale without labeling by detecting the electrochemical signal of the peptides when they pass through the hole. Here, we investigate the influence of nanoscale geometry (conical an…

AmyloidAmyloidAmyloid βSonicationBioengineeringGeometrymacromolecular substances02 engineering and technologyPolyethylene glycol010402 general chemistryFibril01 natural sciencesNanoporeschemistry.chemical_compoundAlzheimer DiseasePEG ratioHumansInstrumentationNanoscopic scaleFluid Flow and Transfer ProcessesAmyloid beta-PeptidesChemistryProcess Chemistry and Technology021001 nanoscience & nanotechnology0104 chemical sciencesKineticsNanopore0210 nano-technologyACS Sensors
researchProduct

N-Terminal amino acid sequence analysis indicates that isolated atrial amyloid is derived from atrial natriuretic peptide

1988

Isolated atrial amyloid, the most frequent senile cardiac amyloid type, was chemically analysed. Amyloid fibrils obtained from a patient (NIP) were extracted and the predominant low-molecular-weight polypeptide (approximately 3.5 kDa, designated ASc2 NIP) was isolated by size exclusion high performance liquid chromatography in 60% formic acid. N-Terminal amino acid sequence analysis of this polypeptide was identical to that of the atrial natriuretic peptide alpha-hANP for the first 12 residues determined.

AmyloidAmyloidFormic acidMolecular Sequence DataSize-exclusion chromatographyIsolated atrial amyloidHigh-performance liquid chromatographyPathology and Forensic Medicinechemistry.chemical_compoundAtrial natriuretic peptidechemistryBiochemistrymental disordersHumansNIPFemaleAmino Acid SequencePeptide sequenceAtrial Natriuretic FactorAgedVirchows Archiv B Cell Pathology
researchProduct

Design and synthesis of new trehalose-conjugated pentapeptides as inhibitors of Aβ(1-42) fibrillogenesis and toxicity

2009

Aggregation of the amyloid A? peptide and its accumulation into insoluble deposits (plaques) are believed to be the main cause of neuronal dysfunction associated with Alzheimer's disease (AD); small molecules that can interfere with the A? amyloid fibril formation are therefore of interest for a potential therapeutic strategy. Three new trehalose-conjugated peptides of the well known ?-sheet breaker peptide iA?5p,were synthesized. The disaccharide was covalently attached to different sites of the LPFFD peptide chain, i.e. at the N-terminus, C-terminus or at the Asp side chain. CD spectroscopy in different solvents was used to assess changes in the peptide conformation of these compounds. Th…

AmyloidCell SurvivalPeptideMicroscopy Atomic ForceBiochemistryMass Spectrometrychemistry.chemical_compoundbeta-sheet breaker peptideStructural BiologySFMmental disordersDrug DiscoveryAnimalsbeta-sheet breaker peptidesMolecular BiologyCells CulturedChromatography High Pressure LiquidtrehaloseCerebral CortexPharmacologychemistry.chemical_classificationthioflavin Tbeta-amyloidOrganic ChemistryP3 peptideFibrillogenesisGeneral MedicineTrehaloseSmall moleculeGlycopeptideNeuronal culturesRatsPeptide Conformationneuronal cultureBiochemistrychemistryMolecular MedicineAmyloid-betaPeptidesJournal of Peptide Science
researchProduct

Polymorphism of amyloid-beta fibrils and its effects on human erythrocyte catalase binding.

2009

The Alzheimer's amyloid-beta (Abeta) peptide exists as a number of naturally occurring forms due to differential proteolytic processing of its precursor molecule. Many of the Abeta peptides of different lengths form fibrils in vitro, which often show polymorphisms in the fibril structure. This study presents a TEM based analysis of fibril formation by eighteen different Abeta peptides ranging in length from 5 to 43 amino acids. Spectrophotometric analysis of Congo red binding to the fibrillar material has been assessed and the binding of human erythrocyte catalase (HEC) to Abeta fibrils has also been investigated by TEM. The results show that a diverse range of Abeta peptides form fibrils a…

AmyloidErythrocytesGeneral Physics and AstronomyPeptidemacromolecular substancesPlasma protein bindingFibrilchemistry.chemical_compoundMicroscopy Electron TransmissionStructural BiologyHumansGeneral Materials Sciencechemistry.chemical_classificationbiologyStaining and LabelingCongo RedCell BiologyCatalaseIn vitroAmino acidCongo redPolymorphism (materials science)BiochemistrychemistryCatalaseSpectrophotometrybiology.proteinProtein BindingMicron (Oxford, England : 1993)
researchProduct

Negative staining across holes: application to fibril and tubular structures.

2007

The negative staining technique, when used with holey carbon support films, presents superior imaging conditions than is the case when samples are adsorbed to continuous carbon films. A demonstration of this negative staining approach is presented, using ammonium molybdate in combination with trehalose, applied to several fibrillar and tubular samples. Fibrils formed from the amyloid-beta peptide and the protease inhibitor pepstain A spread very well unsupported across holes and the different polymorphic fibril forms can be readily assessed. However, tubular forms of amyloid-beta have a tendency to be flattened, due to surface tension forces prior to and during specimen drying. Sub-fibril a…

AmyloidMaterials scienceGeneral Physics and Astronomychemistry.chemical_elementFibrilNegative Stainingchemistry.chemical_compoundFerrihydriteMicroscopy Electron TransmissionStructural BiologyIron-Binding ProteinsPepstatinsAnimalsHumansNanotechnologyGeneral Materials ScienceAmmonium molybdateMolybdenumAmyloid beta-PeptidesProteinsTrehaloseCell BiologyDNATrehaloseNegative stainCarbonStainingRatsCrystallographyCarbon filmchemistryBiophysicsCollagenPeptidesCarbonMicron (Oxford, England : 1993)
researchProduct

Structural analysis of copper(I) interaction with amyloid β peptide

2019

Abstract The N-terminal fragment of Aβ (β = beta) peptide is able to bind essential transition metal ions like, copper, zinc and iron. Metal binding usually occurs via the imidazole nitrogens of the three His residues which play a key role in the coordination chemistry. Among all the investigated systems, the interaction between copper and Amyloid β assume a biological relevance because of the interplay between the two copper oxidation states, Cu(II) and Cu(I), and their involvement in redox reactions. Both copper ions share the ability to bind Amyloid β. A huge number of investigations have demonstrated that Cu(II) anchors to the N-terminal amino and His6, His13/14 imidazole groups, while …

AmyloidSilverCoordination spherechemistry.chemical_elementPeptide010402 general chemistrySilver(I)01 natural sciencesBiochemistryRedoxCoordination complexInorganic ChemistryMetalchemistry.chemical_compoundCoordination ComplexesImidazoleHistidineAmino Acid SequenceHistidinechemistry.chemical_classificationAmyloid beta-Peptides010405 organic chemistryChemistryStructureCopperPeptide Fragments0104 chemical sciencesCrystallographyCoordinationvisual_artvisual_art.visual_art_mediumCopper(I)CopperProtein BindingJournal of Inorganic Biochemistry
researchProduct

Generation of TCR-Engineered T Cells and Their Use To Control the Performance of T Cell Assays

2015

Abstract The systematic assessment of the human immune system bears huge potential to guide rational development of novel immunotherapies and clinical decision making. Multiple assays to monitor the quantity, phenotype, and function of Ag-specific T cells are commonly used to unravel patients’ immune signatures in various disease settings and during therapeutic interventions. When compared with tests measuring soluble analytes, cellular immune assays have a higher variation, which is a major technical factor limiting their broad adoption in clinical immunology. The key solution may arise from continuous control of assay performance using TCR-engineered reference samples. We developed a simp…

AnalyteT-LymphocytesT cellImmunologyReceptors Antigen T-CellGene ExpressionT-Cell Antigen Receptor SpecificityComputational biologyImmunologic TestsBiologyImmune systemClinical decision makingHLA AntigensmedicineHumansImmunology and AllergyT-cell receptorLimitingmedicine.anatomical_structureImmunologyImmunotherapyProtein MultimerizationSources of errorGenetic EngineeringPeptidesFunction (biology)The Journal of Immunology
researchProduct

Thermodynamic Study of Small Hydrophobic Ions at the Water–Lipid Interface

2001

Abstract The thermodynamics of binding of two small hydrophobic ions such as norharman and tryptophan to neutral and negatively charged small unilamellar vesicles was investigated at pH 7.4 using fluorescence spectroscopy. Vesicles were formed at room temperature from dimyristoyl phosphatidylcholine (DMPC) or DMPC/dimyristoylphosphatidic acid and DMPC/dimyristoylphosphatidylglycerol. The changes in fluorescence properties were used to obtain association isotherms at variable membrane surface negative charge and at different ionic strengths. The binding of both ions was found to be quantitatively enhanced as the percentage of negative phospholipid increases in the membrane. Also, a decrease …

Analytical chemistryPhospholipidPhosphatidic AcidsIonic bondingBiomaterialschemistry.chemical_compoundColloid and Surface ChemistryIon bindingElectrochemistryLipid bilayerUnilamellar LiposomesIonsChromatographyVesicleTryptophanBinding constantSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsPartition coefficientHarminechemistryPartition equilibriumThermodynamicslipids (amino acids peptides and proteins)DimyristoylphosphatidylcholineHydrophobic and Hydrophilic InteractionsCarbolinesJournal of Colloid and Interface Science
researchProduct

Common genetic denominators for Ca++-based skeleton in Metazoa: role of osteoclast-stimulating factor and of carbonic anhydrase in a calcareous spong…

2012

Calcium-based matrices serve predominantly as inorganic, hard skeletal systems in Metazoa from calcareous sponges [phylum Porifera; class Calcarea] to proto- and deuterostomian multicellular animals. The calcareous sponges form their skeletal elements, the spicules, from amorphous calcium carbonate (ACC). Treatment of spicules from Sycon raphanus with sodium hypochlorite (NaOCl) results in the disintegration of the ACC in those skeletal elements. Until now a distinct protein/enzyme involved in ACC metabolism could not been identified in those animals. We applied the technique of phage display combinatorial libraries to identify oligopeptides that bind to NaOCl-treated spicules: those oligop…

Anatomy and PhysiologyMarine and Aquatic Scienceslcsh:MedicineBiochemistryCalcium Chloridechemistry.chemical_compoundMolecular Cell BiologySycon raphanuslcsh:ScienceCarbonic AnhydrasesSclerocytechemistry.chemical_classification0303 health sciencesMultidisciplinaryCalcareous spongebiology030302 biochemistry & molecular biologyIntracellular Signaling Peptides and ProteinsRecombinant ProteinsAmorphous calcium carbonatePoriferaEnzymesChemistrymedicine.anatomical_structureBiochemistryMedicineOligopeptidesResearch ArticleBiotechnologyDNA ComplementaryMolecular Sequence DataMarine BiologyCalcium Carbonate03 medical and health sciencesSponge spiculeOsteoclastCarbonic anhydraseChemical BiologymedicineAnimalsAmino Acid SequenceBiology030304 developmental biologySequence Homology Amino AcidEvolutionary Developmental Biologylcsh:Rbiology.organism_classificationEnzymechemistryEarth Sciencesbiology.proteinCalciumlcsh:QPeptidesPhysiological ProcessesDevelopmental BiologyPLoS ONE
researchProduct