Illustration of the Multivalent Evolved DNA-based SUpramolecular Assemblies (MEDUSA), shown in white, interacting with a target protein (pink). (Credit: 2025 PBL EPFL CC BY SA 4.0)

Inspired by the way viruses attach to cells, scientists have developed a method for engineering ultra-selective aptamers. These synthetic molecules bind to specific targets like viral spike proteins, making them useful for biomedical diagnostics and treatments.

The key to developing trimeric binders is the scaffold: a molecular structure around which three binding units naturally assemble. In their experiments, the researchers developed their scaffold based on the geometry of the SARS-CoV-2 spike protein. By adding these tailored scaffolds to their aptamer library, the team was able to bias the sequence space toward trimeric candidates that would bind functionally to the target interface right from the start.

Once a first batch of binders is identified, candidates with increasing affinity for their target are developed through an iterative process of selection and amplification called ‘evolution’.

Although designing new scaffolds can take a matter of hours, the evolution process can take weeks. Looking ahead, the research team aims to shorten this timeframe to better suit the needs of biomedical diagnostics and therapeutics.

Another goal is to develop multimeric binders targeting pathogens with even more complex configurations, like Dengue fever (six binding subunits) or anthrax (seven).

Source 

Topics:
Diagnostics Drug Delivery Medical Product Development

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