algorithms developed at the University of Michigan can highlight problem areas in antibodies that make them prone to binding non-target molecules.
Unfortunately, antibodies designed to bind their specific antigens very strongly and quickly can also bind non-antigen molecules, which removes the antibodies before they target a disease. Such antibodies are also prone to binding with other antibodies of the same type and, in the process, forming thick solutions that don't flow easily through the needles that deliver antibody drugs.
An antibody that doesn't check all three boxes is unlikely to become a successful drug, but many clinical-stage antibodies can't. In their new study, Tessier's team measured the activity of 80 clinical-stage antibodies in the lab and found that 75% of the antibodies interacted with the wrongthat constitute an antibody, and in turn the antibody's 3D structure, could prevent antibodies from misbehaving because an antibody's structure determines what it can bind.