We analyzed the human genome to find proteins naturally capable of self-assembling into stable structures, encapsulating their own genes and bringing those genes to other cells or parts of the human genome.
We demonstrated that these proteins could form solid, stable nanoparticles through a guided process, leveraging specific genetic circuits. Furthermore, they proved capable of interacting seamlessly with human cells, paving the way for a groundbreaking, biologically inspired delivery platform.
We analyzed these proteins in depth, studying their natural functions and structures to engineer them for therapeutic applications. Our goal was to remove unnecessary natural functions while adapting key properties to enhance their performance.
By refining their design, we transformed these proteins so that, instead of encapsulating their own genetic material, they now efficiently carry and protect our molecules of interest. Additionally, we optimized their natural encapsulation capacity, ensuring a more efficient and precise delivery system.
The result is a synthetic core composed of human protein sequences that self-assemble into nanoparticles. These nanoparticles efficiently encapsulate therapeutic cargo, overcoming immunogenicity, toxicity, and lack of control—key challenges of conventional delivery systems.
