Intracellular protein delivery is a promising avenue for biological imaging, genome engineering, and therapeutic development. The major challenge of effective delivery is to keep functional proteins in an active conformation at their site of action. Endosomal entrapment and protease-mediated degradation make standard protein delivery strategies inefficient. We have recently fabricated self-assembled superstructures through co-engineering of proteins and nanoparticles for direct cytosolic delivery to cells. These superstructures were formed by electrostatic interaction between glutamic acid-tagged recombinant proteins (E-tagged proteins) and positively-charged arginine gold nanoparticles (ArgNP). These assemblies fuse with the cell membrane, releasing the E-tagged proteins directly into the cytosol. Significantly, the E-tagged proteins retained activity after delivery, as demonstrated by gene editing of Cas9 proteins. We will discuss the use of this delivery platform for protein and CRISPR based therapeutics for B cell lymphoma.

Self-assembly of nanoparticle-protein superstructures for the direct cytosolic protein delivery to lymphoma B cells

256th National Meeting (2018)

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