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Related Experiment Video

Updated: Jun 7, 2026

The Nijmegen Hemostasis Assay: Simultaneous Fluorogenic Measurement of Thrombin and Plasmin Generation in a Single Well
08:01

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Published on: February 27, 2026

Time-resolved fluorescence aptamer-based sandwich assay for thrombin detection.

Da-Wei Huang1, Cheng-Gang Niu, Pin-Zhu Qin

  • 1College of Environmental Science and Engineering, Key Laboratory of Environmental Biology and Pollution Control, Ministry of Education, Hunan University, Changsha 410082, PR China.

Talanta
|November 2, 2010
PubMed
Summary

This study introduces a new sensitive method for thrombin detection using a time-resolved fluorescence sensing platform and two thrombin aptamers. The developed system offers a wide dynamic range and low detection limit for accurate protein analysis.

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Biotechnology

Background:

  • Thrombin is a key enzyme in blood coagulation, making its accurate detection crucial for diagnosing and monitoring various hemostatic and thrombotic disorders.
  • Existing methods for thrombin detection often face limitations in sensitivity, specificity, or complexity.
  • Aptamers, as synthetic nucleic acid receptors, offer a promising alternative for developing highly specific and sensitive biosensors.

Purpose of the Study:

  • To develop a novel, sensitive, and specific method for thrombin detection using a time-resolved fluorescence sensing platform.
  • To investigate the efficacy of using two distinct thrombin aptamers as capture and detection probes for thrombin quantification.
  • To evaluate the performance of the developed aptasensor in terms of linear dynamic range, detection limit, specificity, and selectivity.

Main Methods:

  • A sandwich assay format was designed utilizing a 15-mer thrombin aptamer as a capture probe immobilized on a glass slide and a 29-mer thrombin aptamer, fluorescently labeled with a europium complex, as the detection probe.
  • Thrombin binding was detected via time-resolved fluorescence intensity, which was found to be directly proportional to thrombin concentration.
  • The aptasensor's specificity was confirmed by demonstrating the retention of thrombin while effectively removing nonspecific proteins through buffer rinsing.

Main Results:

  • The developed aptasensor demonstrated a wide linear dynamic range and a low detection limit for thrombin.
  • The sensing system exhibited satisfactory specificity and selectivity, distinguishing thrombin from other proteins.
  • The results validated the use of aptamers as effective low molecular weight receptors for sensitive and specific protein detection on glass slides.

Conclusions:

  • The novel time-resolved fluorescence sensing platform based on dual thrombin aptamers provides a highly sensitive and specific method for thrombin detection.
  • This aptasensor approach offers a robust and reliable tool for protein analysis in various biological and clinical applications.
  • The study highlights the potential of aptamer-based biosensors for advancing diagnostic capabilities in hemostasis and thrombosis research.