Diabodies are bivalent and mono or bispecific antibody fragments currently used in diagnostics and as cancer therapeutics.1,2 These fragments have two outward facing binding domains in a back-to-back conformation. Structural analysis suggests that diabodies possess conformational flexibility, which may impact on their function and stability. We are using protein engineering and computational approaches in order to explore diabody dynamics with the aim of modulating their conformational properties and thus potential application.
Kim, J. H. et al (2016). "Crystal structures of mono- and bi-specific diabodies and reduction of their structural flexibility by introduction of disulfide bridges at the Fv interface." Sci Rep 6: 34515.