Antibody-drug conjugates are emerging as a frontrunner in precision targeted therapeutics. However, this capability is still beyond the ability of most academic laboratories. The primary reason for this is the need to identify a precise binding site on the constant region of the antibody (Fc) for the drug molecule to be conjugated, while not affecting the ability of the variable region (Fv) of the antibody to bind to its target. Additionally, the maximum number of drug molecules that can be loaded on a single antibody is nominally 1-3.
A solid nanoparticle core overcomes these hurdles by loading the antibody and the drug molecules independent of each other on the surface. A single nanoparticle of ~15 nm in diameter can easily hold up to 10 antibodies and a few 100 small drug molecules on its surface.
We are currently working with multiple collaborators to provide them with nanoparticles that are tagged with dual antibodies (targeting and therapeutic), antibody/oligonucleotide combinations (siRNA, miRNA, shRNA), and targeting peptide/oligonucleotide combinations.
All nanoparticles are characterized using transmission electron microscopy (TEM), dynamic light scattering (DLS) and zeta potential. Surface functional groups are characterized using nuclear magnetic resonance (NMR) and Fourier transform infra-red spectroscopy (FT-IR).