Enlightening the Fcab-antigen interaction via X-ray crystallography & solution studies

The modular nature of antibodies allows the design of antibody-related formats with tailored characteristics. The antibody’s Fc part, encompassing the effector functions, represents an attractive scaffold for engineering therapeutic molecules as demonstrated by the generation of Fcabs (Fc domain with antigen-binding sites). By engineering the C-terminal loops (AB, CD and EF loop) in the CH3 domains, two antigen binding sites can be inserted in close proximity. 

The study presented in this webinar deals with the determination of the first X-ray structures of three Fcabs that differ in loop design, specificity, affinity and thermal stability and reveals their overall structural integrity and native fold. 

Furthermore, by investigation of the interaction of these Fcabs with their respective antigens (HER2 or VEGF) using a set of complementary techniques (X-ray crystallography, size exclusion chromatography combined with multi-angle light scattering [SEC-MALS], isothermal titration calorimetry [ITC], fluorescence correlation spectroscopy [FCS]), insights into the binding modes and binding stoichiometries were gained.



May 15 2018 - May 15 2018
10:30 - 11:30
(GMT-05:00) Eastern [US & Canada]
Event type:
Webinar - Live
Size Exclusion Chromatography (SEC) 
X-ray Diffraction (XRD) 
Isothermal Titration Calorimetry (ITC)


Elisabeth Lobner is a post-doctoral researcher in the Department of Biotechnology at the University of Natural Resources and Life Sciences (BOKU) in Vienna, Austria. Her current research mainly focuses on the application of animal cell factories, particularly on difficult-to-express proteins. During her 4-year tenure as a PhD student at the Department of Chemistry (BOKU) in cooperation with F-star Biotechnology Ltd., she investigated the interaction between certain antibody-fragments and their respective antigens. Before this, Elisabeth completed her Master’s degree in biotechnology at BOKU.