Decoding aptamer-protein binding kinetics for continuous biosensing using single-molecule techniques.

ABSTRACT: Continuous biosensing provides real-time information about biochemical processes and holds great potential for health monitoring. Aptamers have emerged as promising alternatives over traditional biorecognition elements. However, the underlying aptamer-target binding interactions are often poorly understood. Here, we present a technique that can decode aptamer-protein binding interactions at the single-molecule level. We demonstrate that our single-molecule assay is able to decode the underlying binding kinetics of aptamers despite their similar binding affinity. Guided by computational simulations and validated with quartz crystal microbalance experiments, we show that the quantitative insights generated by this single-molecule technique enabled the rational understanding of biosensor perf

SUBMITTER: Filius M 

PROVIDER: S-EPMC11827629 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature