Search results for "10019 Department of Biochemistry"

showing 2 items of 2 documents

Carnosine Inhibits Aβ42Aggregation by Perturbing the H-Bond Network in and around the Central Hydrophobic Cluster

2013

Aggregation of the amyloid-β peptide (Aβ) into fibrillar structures is a hallmark of Alzheimer's disease. Thus, preventing self-assembly of the Aβ peptide is an attractive therapeutic strategy. Here, we used experimental techniques and atomistic simulations to investigate the influence of carnosine, a dipeptide naturally occurring in the brain, on Aβ aggregation. Scanning force microscopy, circular dichroism and thioflavin T fluorescence experiments showed that carnosine does not modify the conformational features of Aβ42 but nonetheless inhibits amyloid growth. Molecular dynamics (MD) simulations indicated that carnosine interacts transiently with monomeric Aβ42 by salt bridges with charge…

Circular dichroismMagnetic Resonance Spectroscopy1303 BiochemistryStereochemistryStatic ElectricityCarnosinePeptideMolecular Dynamics SimulationBiochemistryproteinprotein interactionsProtein–protein interactionchemistry.chemical_compoundMolecular dynamicsnutraceutical compounds10019 Department of Biochemistry1312 Molecular BiologyMolecular Biologychemistry.chemical_classificationAmyloid beta-PeptidesDipeptideHydrogen bondOrganic ChemistryIntermolecular forceTemperatureneuroprotective agentHydrogen BondingAlzheimer's diseasePeptide Fragmentsmolecular dynamicscarnosinechemistry1313 Molecular Medicine570 Life sciences; biologyMolecular MedicineHydrophobic and Hydrophilic Interactionsprotein aggregation fibrillogenesis carnosine AFM1605 Organic ChemistryChemBioChem
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A Library-Based Screening Strategy for the Identification of DARPins as Ligands for Receptor-Targeted AAV and Lentiviral Vectors

2021

Delivering genes selectively to the therapeutically relevant cell type is among the prime goals of vector development. Here, we present a high-throughput selection and screening process that identifies designed ankyrin repeat proteins (DARPins) optimally suited for receptor-targeted gene delivery using adeno-associated viral (AAV) and lentiviral (LV) vectors. In particular, the process includes expression, purification, and in situ biotinylation of the extracellular domains of target receptors as Fc fusion proteins in mammalian cells and the selection of high-affinity binders by ribosome display from DARPin libraries each covering more than 1012 variants. This way, DARPins specific for the …

0301 basic medicinelcsh:QH426-470610 Medicine & healthComputational biologyQH426-470BiologyGene deliveryArticleViral vector03 medical and health sciences0302 clinical medicine1311 GeneticsLV10019 Department of Biochemistry1312 Molecular BiologyGeneticsVector (molecular biology)lcsh:QH573-671Molecular Biology030304 developmental biology0303 health sciencesQH573-671lcsh:Cytology10179 Institute of Medical Microbiologyribosome displayCorrectionAAVFusion proteinlcsh:GeneticsCD105NKp46DARPin030104 developmental biologyGluA4DARPin1313 Molecular Medicine030220 oncology & carcinogenesisBiotinylationRibosome displayreceptor-targeted viral vectors570 Life sciences; biologyMolecular MedicineAnkyrin repeatCytologyMolecular Therapy - Methods & Clinical Development
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