HOUSTON, Aug. 24 (Xinhua) -- Researchers in Rice University, Texas, have developed a method to efficiently modify natural antibodies that can deliver drugs to target cells.
According to a news release by Rice University on Thursday, Rice chemist Zachary Ball and graduate student and lead author Jun Ohata discovered that rhodium, a rare transition metal, can be a useful element in the design and preparation of antibody drug conjugates (treatments) that have become a standard tool for targeted delivery of drugs such as chemotherapeutics.
They developed a unique multimetallic protein that acts like an enzyme to catalyze the action of a wide variety of antibodies. The simple process will allow labs to test the relative function of a variety of antibody sources and antigen targets to see which will work best on a tumor cell.
The key is to have three rhodium complexes attached to specific sites of a protein that binds to the constant (Fc) antibody region. Once bound, this multimetallic peptide catalyzes site-specific attachment of therapeutic agents with minimal disruption to the antibody itself. The lab tested its complexes on breast cancer cells and confirmed that the modified antibodies retained their antigen-binding properties.
"We think of this as the frontier of chemical selectivity," Ball said. "We've got this massive molecule that weighs 150,000 kilodaltons. How do we find one hydroxyl group in that massive structure and do chemistry on it? These are the kind of fundamental things that chemists love to think about."
Ball's lab is beginning to work with Texas Medical Center collaborators to test the new catalyst. "We want to get these in the hands of clinicians and drug development people to see what these conjugates can do," he said.
The research appears in the Journal of the American Chemical Society.
