Search results for "PEPTIDE"

showing 10 items of 4589 documents

Targeting Alzheimer’s disease with multimodal polypeptide-based nanoconjugates

2021

LRP1-targeted St-Cl–polyglutamate conjugates as multivalent neuroprotective/neurotrophic therapeutics for Alzheimer’s disease.

Alzheimer’s disease (AD)Mice TransgenicNanoconjugatesHippocampal formationHippocampusNeuroprotectionAD treatmentMice03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAlzheimer DiseaseBisdemethoxycurcuminAnimalsOlfactory memoryResearch Articles030304 developmental biology0303 health sciencesAmyloid beta-PeptidesMultidisciplinaryPolyglutamatebiologySciAdv r-articlesLife Sciences3. Good healthOlfactory bulbDisease Models AnimalApplied Sciences and Engineeringchemistrybiology.proteinNeuroscience030217 neurology & neurosurgeryNanoconjugatesResearch ArticleNeurotrophinScience Advances
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Biomarkers Related to Synaptic Dysfunction to Discriminate Alzheimer’s Disease from Other Neurological Disorders

2022

Recently, the synaptic proteins neurogranin (Ng) and α-synuclein (α-Syn) have attracted scientific interest as potential biomarkers for synaptic dysfunction in neurodegenerative diseases. In this study, we measured the CSF Ng and α-Syn concentrations in patients affected by AD (n = 69), non-AD neurodegenerative disorders (n-AD = 50) and non-degenerative disorders (n-ND, n = 98). The concentrations of CSF Ng and α-Syn were significantly higher in AD than in n-AD and n-ND. Moreover, the Aβ42/Ng and Aβ42/α-Syn ratios showed statistically significant differences between groups and discriminated AD patients from n-AD patients, better than Ng or α-Syn…

Alzheimer’s disease; biomarkers; neurogranin; α-synucleinAmyloid beta-PeptidesneurograninOrganic ChemistrybiomarkersNeurodegenerative Diseasestau ProteinsGeneral MedicineCatalysisSettore MED/01 - Statistica MedicaComputer Science ApplicationsInorganic Chemistryα-synucleinAlzheimer DiseaseFluorodeoxyglucose F18alpha-SynucleinHumansCognitive DysfunctionSettore MED/26 - NeurologiaPhysical and Theoretical ChemistryAlzheimer’s diseaseMolecular BiologySpectroscopyInternational Journal of Molecular Sciences; Volume 23; Issue 18; Pages: 10831
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Identification of a new series of amides as non-covalent proteasome inhibitors

2014

Proteasome inhibition has emerged as an important therapeutic strategy for the treatment of multiple myeloma (MM) and some forms of lymphoma, with potential application in other types of cancers. 20S proteasome consists of three different catalytic activities known as chymotrypsin-like (ChT-L), trypsin-like (T-L), and, post-glutamyl peptide hydrolyzing (PGPH) or caspase-like (C-L), which are located respectively on the β5, β2, and β1 subunits of each heptameric β rings. Currently a wide number of covalent proteasome inhibitors are reported in literature; however, the less widely investigated non-covalent inhibitors might be a promising alternative to employ in therapy, because of the lack o…

AmideMagnetic Resonance SpectroscopyStereochemistryProtein subunitPeptideMolecular Docking SimulationDrug DiscoverymedicineHumansProteasome inhibitorDocking studiesMultiple myelomaPharmacologychemistry.chemical_classificationOrganic ChemistryGeneral Medicinemedicine.diseaseAmidesYeastMolecular Docking SimulationchemistryProteasomeBiochemistryNon-covalent inhibitorDocking (molecular)Covalent bondProteasome Inhibitors
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Faldaprevir (BI 201335), BI 207127 and ribavirin oral therapy for treatment-naive HCV genotype 1: SOUND-C1 final results

2013

Background Faldaprevir (BI 201335) and deleobuvir (BI 207127) are direct-acting antiviral agents under development for the treatment of chronic HCV infection. This article describes the final results of the Phase Ib SOUND-C1 study that evaluated the interferon-free oral combination of faldaprevir, deleobuvir and ribavirin in 32 treatment-naive patients infected with HCV genotype 1. Methods Patients were randomized to receive deleobuvir 400 mg ( n=15) or 600 mg ( n=17) three times daily plus faldaprevir 120 mg once daily and weight-based ribavirin for 4 weeks. Interferon-free therapy was followed by response-guided faldaprevir plus pegylated interferon-α2a/ribavirin to week 24 or 48. Results…

Aminoisobutyric AcidsProline[SDV]Life Sciences [q-bio]610 Medicine & healthHepacivirusAntiviral AgentsDrug Administration SchedulePolyethylene GlycolsTherapy naive03 medical and health scienceschemistry.chemical_compound0302 clinical medicineHcv genotype 1LeucineRibavirinMedicine2736 Pharmacology (medical)Pharmacology (medical)Oral therapy030304 developmental biologyPharmacology0303 health sciencesbusiness.industryRibavirinDeleobuvirInterferon-alpha2725 Infectious DiseasesHepatitis C ChronicViral LoadVirologyRecombinant Proteins3. Good healthThiazolesInfectious DiseasesTreatment Outcome10219 Clinic for Gastroenterology and Hepatology3004 PharmacologychemistryAcrylatesFaldaprevirQuinolines030211 gastroenterology & hepatologyBenzimidazolesDrug Therapy CombinationbusinessOligopeptides
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Immobilization of functionalized lipids in a random poly(methacrylate) copolymer monolayer

1995

It is shown that a monolayer of random poly(methacrylate) copolymer with a hydrophobic and a hydrophilic substituent exhibits a transition from the fluid to amorphous state. Above this transition any amphiphilic molecules mixed with the monolayer are immobile. Furthermore, such functionalized lipids are immobilized in the monolayer during the Langmuir-Blodgett transfer. The hydrophilic head-groups of the biotin-lipids remain on the formerly water-adjacent side of the monolayer, even if this side is exposed to air

Amphiphilic moleculeMaterials scienceMethacrylate copolymerMechanical EngineeringSubstituentMethacrylatePoly methacrylateAmorphous solidchemistry.chemical_compoundchemistryMechanics of MaterialsPolymer chemistryMonolayerCopolymerlipids (amino acids peptides and proteins)General Materials ScienceAdvanced Materials
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Emerging contributions of formyl peptide receptors to neurodegenerative diseases.

2021

Abstract Inflammation is a central element of many neurodegenerative diseases. Formyl peptide receptors (FPRs) can trigger several receptor-dependent signal transduction pathways that play a key role in neuroinflammation and neurodegeneration. They are chemotactic receptors that help to regulate pro- and anti-inflammatory responses in most mammals. FPRs are primarily expressed in the immune and nervous systems where they interact with a complex pattern of pathogen-derived and host-endogenous molecules. Mounting evidence points towards a contribution of FPRs – via neuropathological ligands such as Amyloid beta, and neuroprotective ligands such as Humanin, Lipoxin A4, and Annexin A1 – to mult…

Amyloid beta-PeptidesClinical BiochemistryNeurodegenerationChemotaxisNeurodegenerative DiseasesBiologymedicine.diseaseLigandsBiochemistryNeuroprotectionReceptors Formyl PeptideNeuroinflammatory DiseasesmedicineFunctional selectivityAnimalsHumansSignal transductionMolecular BiologyCentral elementNeuroscienceNeuroinflammationHumaninBiological chemistryReferences
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Genistein effect on cognition in prodromal Alzheimer's disease patients : the GENIAL clinical trial

2022

Background: Delaying the transition from minimal cognitive impairment to Alzheimer’s dementia is a major concern in Alzheimer’s disease (AD) therapeutics. Pathological signs of AD occur years before the onset of clinical dementia. Thus, long-term therapeutic approaches, with safe, minimally invasive, and yet efective substances are recommended. There is a need to develop new drugs to delay Alzheimer’s dementia. We have taken a nutritional supplement approach with genistein, a chemically defned polyphenol that acts by multimodal specifc mechanisms. Our group previously showed that genistein supplementation is efective to treat the double transgenic (APP/PS1) AD animal model. Methods: In this…

Amyloid beta-PeptidesSoy isofavonesCognitive NeurosciencePhytoestrogensNeuronesGenisteinCognitive impairmentAmyloid-beta cingulate gyrusCognitionNeurologyAlzheimer DiseaseMalaltiesHumansCognitive DysfunctionNeurology (clinical)
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Cellular Prion Protein Participates in Amyloid-β Transcytosis across the Blood—Brain Barrier

2012

The blood—brain barrier (BBB) facilitates amyloid-β (Aβ) exchange between the blood and the brain. Here, we found that the cellular prion protein (PrPc), a putative receptor implicated in mediating Aβ neurotoxicity in Alzheimer's disease (AD), participates in Aβ transcytosis across the BBB. Using an in vitro BBB model, [125I]-Aβ1–40 transcytosis was reduced by genetic knockout of PrPc or after addition of a competing PrPc-specific antibody. Furthermore, we provide evidence that PrPc is expressed in endothelial cells and, that monomeric Aβ1–40 binds to PrPc. These observations provide new mechanistic insights into the role of PrPc in AD.

Amyloid βanimal diseasesBiologyBrief CommunicationBlood–brain barrierModels BiologicalMiceAlzheimer Diseasemental disordersmedicineAnimalsPrPC ProteinsPrion proteinReceptorCells CulturedAmyloid beta-PeptidesNeurotoxicitymedicine.diseaseMolecular biologyPeptide FragmentsIn vitronervous system diseasesCell biologymedicine.anatomical_structureNeurologyTranscytosisBlood-Brain BarrierGene Knockdown Techniquesbiology.proteinNeurology (clinical)AntibodyTranscytosisCardiology and Cardiovascular MedicineProtein BindingJournal of Cerebral Blood Flow & Metabolism
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The sea urchin embryo: a model to study Alzheimer's beta amyloid induced toxicity.

2009

Abstract Alzheimer’s disease (AD) is the most common form of dementia. The cause of AD is closely related to the accumulation of amyloid beta peptide in the neuritic plaques. The use of animal model systems represents a good strategy to elucidate the molecular mechanism behind the development of this pathology. Here we use the Paracentrotus lividus embryo to identify molecules and pathways that can be involved in the degenerative process. As a first step, we identified the presence of an antigen related to the human APP, called Pl APP. This antigen, after gastrula stage, is processed producing a polypeptide of about 10 kDa. By immunohistochemistry we localized the Pl APP antigen in some ser…

AmyloidAmyloid betaBiophysicsApoptosisBiochemistryNervous SystemParacentrotus lividusAlzheimer Diseasebiology.animalAnimalsHumansSenile plaquesAntigensMolecular BiologySea urchinCaspaseTUNEL assayAmyloid beta-Peptidesbiologybiology.organism_classificationPeptide FragmentsRecombinant ProteinsCell biologyBiochemistryApoptosisCaspasesModels Animalbiology.proteinParacentrotusParacentrotus lividusAmyloid-betaOligomers Fibrillar aggregatesApoptosisAnimal modelArchives of biochemistry and biophysics
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In vitro fibrillogenesis of the amyloid beta 1-42 peptide: cholesterol potentiation and aspirin inhibition.

2002

Understanding the formation of extracellular amyloid neurofibrillar bundles/senile plaques and their role in the development of Alzheimer's disease is of considerable interest to neuroscientists and clinicians. Major components of the extracellular neurofibrillar bundles are polymerized amyloid beta (Abeta) peptides (1-40), (1-42) and (1-43), derived in vivo from the soluble amyloid precursor protein (sAPP) by proteolytic (beta- and gamma-secretase) cleavage. The Abeta(1-42) peptide is widely considered to be of greatest significance in relation to the pathogenesis of Alzheimer's disease. A well-defined ultrastructural characteristic within Alzheimer dense plaques is the presence of helical…

AmyloidAmyloid betaGeneral Physics and AstronomyPeptideFibrilStructural BiologyAlzheimer DiseaseAmyloid precursor proteinAnimalsHumansGeneral Materials ScienceSenile plaqueschemistry.chemical_classificationAmyloid beta-PeptidesbiologyAspirinChemistryP3 peptideFibrillogenesisCell BiologyRatsSphingomyelinsMicroscopy ElectronCholesterolBiochemistrybiology.proteinlipids (amino acids peptides and proteins)PeptidesDimerizationCopperMicron (Oxford, England : 1993)
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