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Triblock PolyA-Mediated Protein Biosensor Based on a Size-Matching Proximity Hybridization Analysis
Yuru Chen1,2, Yanli Wen1, Lele Wang1
1Key Laboratory of Bioanalysis and Metrology for state market regulation, Shanghai Institute of Measurement and Testing Technology, Shanghai 201203, China.
Analytical Chemistry
|April 18, 2024
Summary
Researchers created a novel biosensor using DNA self-assembly to precisely arrange aptamer probes. This enhances biological affinity and improves detection sensitivity for proteins like PDGF-BB in serum.
Area of Science:
- Biomolecular Engineering
- Biosensor Technology
- Surface Chemistry
Background:
- Natural antibodies use multivalency for high affinity.
- Mimicking this on biosensing interfaces for enhanced affinity is challenging.
- Precise spatial arrangement of aptamer probes is key.
Purpose of the Study:
- To develop a novel self-assembly layer (SAM) for controlled aptamer probe organization.
- To construct a "lock-and-key-like" proximity hybridization assay (PHA) biosensor.
- To enhance biological affinity and detection performance through tailored probe spacing.
Main Methods:
- Utilized a triblock polyA DNA self-assembly layer on a gold surface.
- Engineered precise one-to-one spatial proximity of DNA probes.
- Adjusted polyA fragment length to match target protein dimensions.
- Developed a proximity hybridization assay (PHA) biosensor.
Main Results:
- Achieved controllable surface arrangement of aptamer probes.
- Demonstrated enhanced aptamer affinity by tailoring probe distance.
- Reported exceptional specificity and sensitivity in detecting PDGF-BB.
- Validated biosensor performance using human serum samples.
Conclusions:
- The novel SAM provides a versatile interface for proximity assays.
- The biosensor offers significantly improved surface arrangement and detection performance.
- This approach enhances biological affinity and sensing capabilities.
