Our focus is to provide safer cancer therapeutics for indications in which there is a large unmet clinical need. Current indications we are targeting include hematological malignancies with the potential to also treat certain solid tumors through decreasing the toxicity of these chemotherapeutics.
Our expertise is to closely analyze the 3-dimensional structure of proteins, enzymes in particular, and through careful rational structure-based design, introduce minor mutations at the amino acid level that affects the enzymatic activity so as to achieve our desired effect.
One class of enzymes we're focusing on that have proven therapeutics benefits are L-asparaginases, enzymes that hydrolyze the amino acid asparagine into aspartate and ammonia. As a chemotherapeutic, it has revolutionized the treatment of the most common type of pediatric cancer, acute lymphoblastic leukemia (ALL) over the past 50 years.
Unfortunately these enzymes also possess a second activity that in various studies have been linked with toxic side effects. We are engineering a greatly improved version of this drug by eliminating the side activity, resulting in a significantly safer therapeutic that will be able to treat patients previously not able to take this life-saving drug.
In this way, not only will more patients be able to be treated with this therapeutic, but the suffering of many patients taking this drug will be greatly decreased compared to those burdened by the side effects of the currently available versions of this drug.
We are engineering safer drugs to help people when they need it most.