Peptides generally exhibit higher speci!city, lower immunogenicityand fewer side effects than common compounds. One of the majordrawbacks of peptide drugs is that they have a relative short half-lifedue to natural degradation or enzymatic hydrolysis. Fortunately, somecurrent peptide modi!cation methods have been used to partiallyovercome this problem. In this study, we added a TAT transmembraneelement to the N-terminal of PDHPS1, TAT-PDHPS1 was not onlyhighly soluble in water, but also had a longer half-life than the originalsequence. In addition, the optimized peptide had a stronger inhibitoryeffect on YAP activity. In future, we may continue to try some otherpeptide modi!cation strategies to further improve clinical applicabilityof PDHPS1.