Matrix‐Activated Aptamer Sensors for Human Serum Analysis
Abstract
Owing to their ease of operation, solution‐phase fluorescent sensors hold a crucial position among aptamer‐based detection tools. However, their performance is regularly compromised when exposed to increasing levels of blood fluids, such as human serum, which limits their potential in clinical settings. Here, we introduce a sensing platform that behaves advantageously within this biological medium, leveraging the most abundant proteins in the matrix, namely albumin and immunoglobulin G, as endogenous activators of fluorophore‐labeled aptamers. In the absence of a target, these serum proteins non‐specifically assemble with the aptamer probe in situ. Upon target binding, the aptamer‐protein complexes are disrupted, shifting the equilibria toward the probe unbound to biopolymers. The fluorescence anisotropy readout reveals the system's reactivity to small‐molecule targets, offering the unique ability to provide both enhanced and consistent responses across a range of high serum levels (25%–90%). As the sensor's performance may be sensitive to inter‐sample serum variations, a standard addition calibration approach is used to ensure reliable quantitative analyses. Overall, the proposed strategy addresses substantial serum‐induced perturbations and preserves assay functionality under biologically challenging conditions, thereby establishing a practical framework for extending homogeneous aptamer‐based sensing to clinically relevant blood matrices.
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BibTeX
@article{barbaroux2026matrixactivated,
title = {{Matrix‐Activated Aptamer Sensors for Human Serum Analysis}},
author = {Amandine Barbaroux and Benoit Chovelon and Emmanuelle Fiore and Sebastien Vezirian and Mickael Henry and Marwa Zoubeidi and Maria C Derosa and Corinne Ravelet and Eric Peyrin},
journal = {Angewandte Chemie International Edition},
year = {2026},
month = sep,
doi = {10.1002/anie.3409471},
url = {https://hal.science/hal-05748844v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Matrix‐Activated Aptamer Sensors for Human Serum Analysis
AU - Amandine Barbaroux
AU - Benoit Chovelon
AU - Emmanuelle Fiore
AU - Sebastien Vezirian
AU - Mickael Henry
AU - Marwa Zoubeidi
AU - Maria C Derosa
AU - Corinne Ravelet
AU - Eric Peyrin
PY - 2026
DA - 2026/09/02
JO - Angewandte Chemie International Edition
DO - 10.1002/anie.3409471
UR - https://hal.science/hal-05748844v1
AB - Owing to their ease of operation, solution‐phase fluorescent sensors hold a crucial position among aptamer‐based detection tools. However, their performance is regularly compromised when exposed to increasing levels of blood fluids, such as human serum, which limits their potential in clinical settings. Here, we introduce a sensing platform that behaves advantageously within this biological medium, leveraging the most abundant proteins in the matrix, namely albumin and immunoglobulin G, as endogenous activators of fluorophore‐labeled aptamers. In the absence of a target, these serum proteins non‐specifically assemble with the aptamer probe in situ. Upon target binding, the aptamer‐protein complexes are disrupted, shifting the equilibria toward the probe unbound to biopolymers. The fluorescence anisotropy readout reveals the system's reactivity to small‐molecule targets, offering the unique ability to provide both enhanced and consistent responses across a range of high serum levels (25%–90%). As the sensor's performance may be sensitive to inter‐sample serum variations, a standard addition calibration approach is used to ensure reliable quantitative analyses. Overall, the proposed strategy addresses substantial serum‐induced perturbations and preserves assay functionality under biologically challenging conditions, thereby establishing a practical framework for extending homogeneous aptamer‐based sensing to clinically relevant blood matrices.
SN - 1433-7851
SN - 1521-3773
ER -