Monoclonal antibodies, or mAbs, are used to treat cancer, autoimmune disorders, and infectious diseases. However, to function properly, these molecules need to maintain a specific structure. FSU’s Christian Bleiholder has found that the monoclonal antibody NISTmAb retains its structure even if the sugar molecules attached to it are changed. “Understanding how sugar molecules influence how monoclonal antibodies behave has been a long-standing challenge in biotherapeutics.”

Bleiholder worked with collaborators at Bruker Daltonics to develop a patented technique called tandem-trapped ion mobility spectrometry, or Tandem-TIMS, that allowed them to preserve the molecules’ structure while studying how their shape changes under different conditions. The team confirmed that structural variations among antibody populations are not influenced by glycosylation, a process in which sugar molecules attach to other molecules.

• Christian Bleiholder