A new group of antibody–drug conjugates (ADCs) has been developed by the research team from The Scripps Research Institute (TSRI) using an adaptable “double decker” technology that binds a drug and antibodies together to generate highly effective pharmaceuticals for the cancer treatment. The new ADC technique advances a category of pharmaceuticals that utilize antibodies to selectively carry drugs to cancer cells without damaging healthy cells and tissues.
Christoph Rader, an Associate Professor, said, “Our new ADCs are developed something similar to a double-decker bus. The targeting antibody acts as the upper deck that fastens onto a cancer cell, whereas the catalytic antibody acts as a lower deck that holds the drug. This is among the stimulating application of an extremely adaptable class of catalytic antibodies formerly developed by Richard A. Lerner and Carlos F. Barbas III of TSRI in the 1990s.”
This new technology dubbed as a dual variable domain antibody–drug conjugates (DVD–ADCs). Essentially, antibodies are the bigger immune system proteins that identify distinctive molecular markers existing on cancer cells known as tumor antigens. Antibodies, on their own, are generally not powerful enough to destroy cancer. Nevertheless, what makes them the ideal carriers for drug delivery directly to cancer cell is their high specificity for tumor antigens.
The new technology was used against multiple myeloma, non-Hodgkin lymphoma, & HER2-driven breast cancer and was found to be highly potent against all 3 cancer types in the animal as well as cell model experiments.
Radar explained, not only is the new DVD–ADC is highly proficient, but it uses a modular congregation, which makes it comparatively easy to implement to diverse cancers and probably to other diseases. Alex Nanna, a Graduate Student, said, “The benefit is we can create ADCs at a rapid rate in one step. The DVD-ADC set-up brings everything collectively in a very competent manner.”
The DVD–ADCs take benefit of a strangely reactive amino acid residue, catalytic antibody’s natural lysine. Radar said, “We can fasten drugs with great stability and precision to this residue and, furthermore, we can utilize it to keep an eye on attachment as the antibody drops its catalytic activity on the attachment of the drug to lysine. It is a very fresh and distinctive approach to substantiate successful ADC creation.”
The technology also removes the requirement of antibody purification during primary production, delaying that process till the ADC is pulled together. Radar said, “From a production viewpoint, this is a significant advantage.”
