Engineered High Affinity IGF1R Imaging Agents from the Novel WNM Protein Scaffold

Abstract

With the support of the Undergraduate Research Opportunities Program (UROP), I set out to construct a novel imaging agent using the WNM scaffold. The WNM protein, based off the T7 phage protein Gp2, was identified earlier for its high β-sheet character, small size (WT: 64 amino acids), and loop regions in the secondary structure capable of binding, making it an ideal candidate for a molecular imaging probe. Using this basic scaffold, I selectively evolved this protein to exhibit high-affinity binding to the protein receptor IGF1R, a marker commonly overexpressed in a number of carcinomas. The final product produced in the time allotted by the UROP was not sufficient to be tested in a biodistribution model, but only requires minimal refinement to reach a final binder.