Particle.news

Download on the App Store

EPFL’s MEDUSA Technique Yields Aptamers With Up to 1,000-Fold Stronger Viral Binding

Successful use of geometry-based molecular scaffolds to assemble trimeric aptamers around the SARS-CoV-2 spike protein paves the way for AI-driven expansion to more complex pathogens.

Image
Image

Overview

  • EPFL’s Programmable Biomaterials Lab developed the MEDUSA platform to generate trimeric aptamers by organizing three binding units on protein-specific molecular scaffolds.
  • When targeting the SARS-CoV-2 spike protein, MEDUSA-derived aptamers showed 10 to 1,000-fold stronger binding affinity than conventional monovalent binders.
  • The multimeric assemblies also demonstrated markedly improved specificity, a key advantage for accurate diagnostics and antiviral therapies.
  • Although scaffold design takes mere hours, the evolutionary selection process to optimize binding can span several weeks, indicating a potential bottleneck for rapid clinical use.
  • Researchers plan to apply MEDUSA to pathogens with more elaborate subunit architectures like Dengue and anthrax and to harness generative AI for faster aptamer discovery.