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Updated: May 19, 2026

Aptamer-Based Target Detection Facilitated by a 3-Stage G-Quadruplex Isothermal Exponential Amplification Reaction

Aptamer-Based Target Detection Facilitated by a 3-Stage G-Quadruplex Isothermal Exponential Amplification Reaction

Published on: October 6, 2022

GOx signaling triggered by aptamer-based ATP detection.

Sarita Sitaula¹, Shirmir D Branch, Mehnaaz F Ali

¹Department of Chemistry, Xavier University of Louisiana, 1 Drexel Drive, New Orleans, LA 70125, USA.

Chemical Communications (Cambridge, England)

|August 10, 2012

Summary

Aptamer-based adenosine triphosphate (ATP) binding releases the flavin adenine dinucleotide (FAD) co-factor. This release activates the glucose oxidase enzyme (GOx), generating a measurable signal for detection.

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Area of Science:

Biochemistry
Molecular Biology
Biosensors

Background:

Aptamers are short DNA or RNA sequences that bind to specific targets.
Glucose oxidase (GOx) is an enzyme that catalyzes the oxidation of glucose.
Flavin adenine dinucleotide (FAD) is a crucial co-factor for GOx activity.

Purpose of the Study:

To develop a novel biosensor for adenosine triphosphate (ATP) detection.
To investigate the mechanism of aptamer-mediated co-factor release and enzyme activation.

Main Methods:

Utilized aptamers engineered to bind ATP.
Investigated the interaction between aptamers, FAD, and apo-GOx (GOx lacking its co-factor).
Measured the enzymatic activity of GOx upon ATP binding and FAD release.

Main Results:

ATP binding to the aptamer induced the release of the FAD co-factor.
Released FAD reactivated apo-GOx, leading to a measurable enzymatic response.
The system demonstrated sensitivity to varying ATP concentrations.

Conclusions:

Aptamer-controlled FAD release provides a mechanism for 'turn-on' GOx activity.
This approach enables the development of sensitive ATP biosensors.
The findings highlight the potential of aptamer-enzyme interactions in signal generation.