text: Particle Display produces higher yields of higher affinity aptamers in less rounds than conventional selection methods. In this method, libraries of aptamers are separated into aptamer particles and separated by fluorescence-activated cell sorting based on affinity. Only the highest affinity aptamer particles are isolated and sequenced into aptamers. This is an affinity-base selection process that is more efficient than selection methods such as SELEX. Particle display may be a reliable aptamer generation method for E-AB sensors due to the high affinity and specificity of target binding.
  Researchers tackled the challenge of isolating high-affinity aptamers in conventional SELEX by introducing Particle Display System (PDS). Using parallel single-molecule emulsion polymerase chain reaction (PCR) for monoclonal aptamer screening, PDS employs emulsion PCR and droplet digital PCR to prevent by-product propagation and preserve rare high-affinity sequences. The one-particle-one-sequence nature of PDS transforms the DNA-target interaction into a particle-target interaction, enabling swift confirmation of aptamer candidate affinities through fluorescence-activated cell sorting or flow cytometry assays. Unlike conventional SELEX, PDS efficiently segregates aptamers, providing a streamlined and effective method for identifying and isolating high-affinity binders. PDS significantly enhances the efficiency of enriching high-affinity aptamers, achieving this in a single round of screening.
  Particle display yields higher quantities of higher affinity aptamers in fewer rounds compared to conventional selection methods. This method separates aptamer libraries into aptamer particles and employs fluorescence-activated cell sorting to isolate particles based on affinity. Only the highest affinity aptamer particles are isolated and sequenced into aptamers. This affinity-based selection process is more efficient than methods such as SELEX. Particle display may be a reliable aptamer generation method for E-AB sensors due to the high affinity and specificity of target binding