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Updated: Jan 23, 2026

Identifying Protein-protein Interaction Sites Using Peptide Arrays
Published on: November 18, 2014
Structure-based design of potent linear peptide inhibitors of the YAP-TEAD protein-protein interaction derived from
Pascal Furet1, Bahaa Salem1, Yannick Mesrouze1
1Novartis Institutes for BioMedical Research, CH-4002 Basel, Switzerland.
Abstract:
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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