One of the most unique and powerful components of each Trillium Agrisome is its protein shell.
The “programmable” coat surrounds the MV-RNA nanoparticle core, and can consist of single or multiple proteins of nearly any composition. In practice, specific proteins are selected to increase the stability, specificity, deliverability, and efficacy of an Agrisome. For instance, certain proteins are included to broaden the uptake routes, overcome barriers within an insect’s digestive system, or capitalize on a cellular or bio-function of the species.
Just as compelling as the shell’s engineering and capabilities, however, is its ability to self-form – as part of the overall Agrisome molecule – upon the co-expression of the ssRNA nanoparticle core and specified proteins. Specific aptamers are designed into the sequence, which form across the exterior of the nanoparticle core upon post-transcription formation. These aptamers in turn bind to their protein targets to complete the fully-formed, self-assembled Agrisome.
Here’s an overview of that process and some of the key outcomes:
This self-formulating activity has been validated through a number of different types of tests:
Importantly, this aptamer-driven assembly process has demonstrated a highly-significant improvement in binding affinity and enthalpy compared to standard electrostatic-driven methods: