Structure-Based Design of Potent Linear Peptide Inhibitors of the YAP-TEAD Protein-Protein Interaction Derived From the YAP Omega-Loop Sequence

Pascal Furet et al., Bioorganic & Medicinal Chemistry Letters (2019) - PMID: 31235263

Product(s) used in this publication:  Specialty Peptides


The YAP-TEAD protein-protein interaction is a potential therapeutic target to treat cancers in which the Hippo signaling pathway is deregulated. However, the extremely large surface of interaction between the two proteins presents a formidable challenge for a small molecule interaction disrupter approach. We have accomplished progress towards showing the feasibility of this approach by the identification of a 15-mer peptide able to potently (nanomolar range) disrupt the YAP-TEAD interaction by targeting only one of the two important sites of interaction. This peptide, incorporating non-natural amino acids selected by structure-based design, is derived from the Ω-loop sequence 85-99 of YAP.

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