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The phosphoinositide 3-kinases (PI3Ks) are heterodimers consisting of the catalytic subunit p110 and the regulatory subunitp85. The PI3K/Akt pathway is strongly deregulated in breast cancer (BC) representing one of the mechanisms of resistance totherapies. Therefore, the identification of inhibitors of PI3K components represents one of the main goals to produce therapeuticagents. Here, we evaluated the efficacy of a phosphopeptide 1257 (P-1257) that targeting p85 strongly inhibits PI3K activity.We tested the effects of P-1257 administration in vitro and in vivo using BC cells expressing different levels of ErbB-2 andresistant or responsive to Trastuzumab. We demonstrated that inhibition of p85 activity by P-1257 induces cell death andsensitizes JIMT-1 and KPL-4 ErbB-2-overexpressing BC cells to Trastuzumab treatment. It is noteworthy that P-1257 deliveryin vivo by electroporation or liposomes significantly inhibits the proliferation of tumor cells engrafted at subcutaneous andvisceral sites. Overall, our data indicate that the p85 subunit is a valid target for therapeutic approaches and suggest that thestructure of the peptide used in our study could be utilized for the development of novel drugs to apply in combination withtherapies that fail to cure BCs with high PI3K activit

Inhibition of p85, the non-catalytic subunit of phosphatidylinositol 3-kinase, exerts potent antitumor activity in human breast cancer cells