Cambridge, UK | 27th August 2015.


Isogenica and Research Corporation Technologies (RCT) publish paper exemplifying RCT’s proprietary Abdurin therapeutic scaffold displayed on Isogenica’s CIS display platform.

Abdurins are small (12.5kDa) proteins isolated from the CH2 domain of IgG and engineered to be displayed in large libraries to discover binders to target molecules of interest. Abdurins retain a portion of the native Fc receptor binding motif which binds to the neonatal Fc receptor to increase protein half-life and tumour uptake.

In the paper, the authors present data on the construction of a large, diverse, phage-display and in vitro CIS display libraries and the isolation of high affinity binders to a cancer target (membrane-bound ephrin receptor tyrosine kinase class A2, EphA2).

High Affinity Binders to EphA2 Isolated from Abdurin Scaffold Libraries; Characterization, Binding and Tumor Targeting

Christopher Ullman, Pascale Mathonet, Arkadiusz Oleksy, Agata Diamandakis, Licia Tomei, Anna Demartis, Chiara Nardi, Sonia Sambucini, Antonino Missineo, Karen Alt, Christoph E. Hagemeyer, Matt Harris, Amos Hedt, Roland Weis, Kurt R. Gehlsen