Journal of Biological Chemistry · 2017 · 12 citations · 45 references
Life SciencesMolecular BiologyNeuroscienceMolecular EvolutionMolecular NeurobiologyMolecular NeuroscienceLigand BindingNeurotransmissionNucleic Acid Aptamer EvolutionRna EngineeringRna-protein InteractionsSynaptic TransmissionAmpa ReceptorsAptamer SpecificityAptamersKainate ReceptorsRna Aptamer BindingRna Aptamer EvolutionRna AptamersSystematic Evolution Of Ligands By Exponential Enrichment
of ∼5 μm, along with GluA1 and GluA2 AMPA receptor subunits. Of note, its shorter version (55 nt) inhibited both AMPA and kainate receptors. In particular, this shorter aptamer blocked equally potently the activity of both the GluK1 and GluK2 kainate receptors. Using homologous binding and whole-cell recording assays, we found that an RNA aptamer most likely binds to the receptor's regulatory site and inhibits it noncompetitively. Our results suggest the potential of using a single receptor target to develop RNA aptamers with dual activity for effectively blocking both AMPA and kainate receptors.
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