Search results for "SELEX"

showing 3 items of 13 documents

Binding of RNA Aptamers to Membrane Lipid Rafts: Implications for Exosomal miRNAs Transfer from Cancer to Immune Cells

2020

Intraluminal vesicles (ILVs) are released into the extracellular space as exosomes after the fusion of multivesicular bodies (MVBs) with the plasma membrane. miRNAs are delivered to the raft-like region of MVB by RNA-binding proteins (RBPs). RNA loading into exosomes can be either through direct interaction between RNA and the raft-like region of the MVB membrane, or through interaction between an RBP&ndash

liposomesendocrine systemmacromolecular substancesexosomesArticleCatalysisraftslcsh:ChemistryInorganic ChemistryMembrane LipidsMembrane Microdomainsimmune cellsCell Line TumorNeoplasmsmicroRNAHumansRNA aptamersPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologyLipid raftSpectroscopyChemistrySELEXMacrophagesVesicleCell MembraneOrganic ChemistryMultivesicular BodiesRNA-Binding ProteinsRNADendritic CellsGeneral MedicineRaftAptamers NucleotideMicrovesiclesComputer Science ApplicationsCell biologyKiller Cells NaturalMicroRNAslcsh:Biology (General)lcsh:QD1-999Cancer cellmiRNAslipids (amino acids peptides and proteins)Systematic evolution of ligands by exponential enrichmentInternational Journal of Molecular Sciences
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Selection of Membrane RNA Aptamers to Amyloid Beta Peptide: Implications for Exosome-Based Antioxidant Strategies

2019

The distribution of amyloid beta peptide 42 (Aβ42) between model exosomal membranes and a buffer solution was measured. The model membranes contained liquid-ordered regions or phosphatidylserine. Results demonstrated that up to ca. 20% of amyloid peptide, generated in the plasma (or intracellular) membrane as a result of proteolytic cleavage of amyloid precursor proteins by β- and γ-secretases, can stay within the membrane milieu. The selection of RNA aptamers that bind to Aβ42 incorporated into phosphatidylserine-containing liposomal membranes was performed using the selection-amplification (SELEX) method. After eight selection cycles, the pool of RNA aptamers was isol…

liposomesphosphatidylserineAmyloidAmyloid betaPeptideexosomesPhosphatidylserinesExosomeCatalysisAntioxidantsraftsInorganic Chemistrylcsh:Chemistrychemistry.chemical_compoundDown’s syndromeoxidative stressHumansRNA aptamersPhysical and Theoretical ChemistryMolecular Biologylcsh:QH301-705.5Spectroscopychemistry.chemical_classificationAmyloid beta-PeptidesbiologyChemistrySELEXCommunicationOrganic ChemistryCell MembraneSELEX Aptamer TechniqueamyloidGeneral MedicinePhosphatidylserineAptamers NucleotideMicrovesiclesPeptide FragmentsComputer Science ApplicationsMembraneBiochemistrylcsh:Biology (General)lcsh:QD1-999biology.proteinAlzheimer’s diseaseSystematic evolution of ligands by exponential enrichmentInternational Journal of Molecular Sciences
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Structure‐ and Interaction‐Based Design of Anti‐SARS‐CoV‐2 Aptamers

2022

Aptamer selection against novel infections is a complicated and time-consuming approach. Synergy can be achieved by using computational methods together with experimental procedures. This study aims to develop a reliable methodology for a rational aptamer in silico et vitro design. The new approach combines multiple steps: (1) Molecular design, based on screening in a DNA aptamer library and directed mutagenesis to fit the protein tertiary structure; (2) 3D molecular modeling of the target; (3) Molecular docking of an aptamer with the protein; (4) Molecular dynamics (MD) simulations of the complexes; (5) Quantum-mechanical (QM) evaluation of the interactions between aptamer and target with …

oligonukleotiditaptamers fragment molecular orbitals method molecular dynamics SARS-CoV-2 SAXSfragment molecular orbitals methodSARS-CoV-2SELEX Aptamer TechniqueOrganic ChemistryaptamersSARS-CoV-2-virusCOVID-19SAXSGeneral ChemistryAptamers NucleotideMolecular Dynamics Simulationlaskennallinen kemiamolecular dynamicsCatalysislääkesuunnitteluMolecular Docking SimulationSARS-CoV-2 белкиSpike Glycoprotein CoronavirusHumansдизайн аптамеровmolekyylidynamiikkaproteiinitChemistry – A European Journal
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