Phage-displayed combinatorial libraries of non-antibody proteins have been designed to bind an array of protein targets.  The primary application is to identify high affinity binders for purification, co-crystallization or as lead molecules to drug design. Affinity reagents were chosen on their small size, ease of expression in a prokaryotic host and stable scaffold based on a framework of loops amenable to length and sequence variability.   Successful targets include HIV-1 Nef, HIV-1 integrase and membrane- protein ShuA.   High affinity target binding has been demonstrated both on and off phage.  In addition, difficult to crystallize membrane proteins have been successfully targeted.  Ech17 bound to ShuA is currently in co-crystallization trials.  These results demonstrate the diversity of the selected affinity reagents to bind important biological targets as well as difficult to crystallize membrane proteins.

Engineered non-antibody protein scaffolds for molecular recognition

243rd National Meeting (2012)

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