ArticleApplied biochemistry and biotechnology2026
Development of a Thiolated PAMAM-Modified Aptamer-Based Impedimetric Biosensor for Zonulin Measurement as a Biomarker of Intestinal Permeability.
Article in Applied biochemistry and biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Altered intestinal permeability is closely associated with gastrointestinal inflammation, and zonulin/pre-haptoglobin-2 has been investigated as a mediator and biomarker of tight junction regulation. This study describes the development of an aptamer-based electrochemical impedance spectroscopy (EIS) biosensor for zonulin measurement. A 40-nucleotide DNA aptamer candidate, ZON-Apt-40 (5'-GGTTGCGTACGATGGTAGCGTTGACCTGCGTACCAAGTTC-3'), was selected based on its length, balanced GC content, absence of long homopolymeric regions, predicted stem-loop formation, and compatibility with thiol-mediated immobilization. Mfold analysis predicted two low-energy secondary structures; the most stable had a Gibbs free energy of -5.63 kcal/mol and contained an exposed loop/bulge region spanning nucleotides 17-23. A DNA-like three-dimensional model of the aptamer was docked against a human zonulin model, and the predicted binding pose suggested that the exposed loop region interacted with polar and positively charged protein residues. Experimentally, a gold microelectrode was modified with thiolated poly(amidoamine) dendrimer (PAMAM-SH), followed by immobilization of AuNP-conjugated thiolated ZON-Apt-40 and blocking with human serum albumin. FTIR confirmed PAMAM-SH functionalization, whereas cyclic voltammetry and EIS verified stepwise electrode modification. Chronoimpedance measurements identified 200 s as a practical readout time. The sensor exhibited a concentration-dependent EIS response to zonulin, with the calibration equation y = 12.276x + 1509 and R² = 0.9981 ± 0.0012. The calculated limits of detection and quantification were 0.949 and 2.877 ng/mL, respectively. Zonulin-spiked serum samples yielded coefficients of variation of 5.1% and 8.3% at 10 and 50 ng/mL, respectively. Overall, the platform demonstrates preliminary feasibility as a rapid, low-volume, label-free impedimetric aptasensor for zonulin detection; however, further validation using larger clinical sample sets and orthogonal binding assays is required.
Indexed as
Identifiers
42599570What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.