ICE Bioscience Posters

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We present an integrated hit discovery platform for B7‑H3 macrocyclic peptide binder screening that synergizes high‑throughput biophysical screening (SPR, SPS) with phage display technology. State-of-the-art protein structure prediction methods were employed to model the peptide–receptor complex, combined with binding free-energy calculations, thereby enabling the rapid identification and optimization of high-affinity cyclic peptide binders against oncology targets.

Our methodology employs parallel in vitro biophysical assays and phage display library screening. Protein structure prediction tools were also utilized to model the cyclic peptide–receptor complex structure, followed by binding free-energy calculations. The sequences obtained from phage display library screening were ranked and selected based on the Ipae metric and binding free-energy values. Target validation was achieved through engineered recombinant protein constructs (including B7-H3, FAP, EGFR, B7-H4 and GPC3) and isogenic cell lines with uniform target expression. Comprehensive evaluation was performed using modular functional assays measuring binding affinity and cellular internalization kinetics.