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Delft University of Technology

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Sci. Adv., Feb 14 2025, 11 (7) eads9687 | https://doi.org/10.1126/sciadv.ads9687 Decoding aptamer-protein binding kinetics for continuous biosensing using single-molecule techniques

Mike Filius ^{1 †}, Lena Fasching ^{2 †}, Raman van Wee ¹, Alina Y Rwei ^{2 *}, Chirlmin Joo ^{1 3 *}

¹Department of BioNanoScience, Kavli Institute of Nanoscience, Delft University of Technology, 2629 HZ Delft, Netherlands.
²Department of Chemical Engineering, Delft University of Technology, 2629 HZ Delft, Netherlands.
³Department of Physics, Ewha Womans University, Seoul 03760, Republic of Korea.

^†These authors contributed equally

^*Corresponding authors: correspondence to Alina Y Rwei or Chirlmin Joo

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 performance (i.e., the sensitivity and limit of detection). This capability was demonstrated with thrombin as the analyte and the structurally similar aptamers HD1, RE31, and NU172 as the biorecognition elements. This work decodes aptamer-protein interactions with high temporal resolution, paving the way for the rational design of aptamer-based biosensors.

논문정보

형식Research article
게재일2025년 02월 (BRIC 등록일 2025-02-20)
연구진국내(교신)+국외 연구진
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