TRIA-2

TRIA-2 is a potent, selective, and non-covalent small molecule inhibitor of **Ubiquitin-Specific Protease 7 (USP7)**, currently in preclinical development by **Triana Biomedicines**. USP7 is a deubiquitinating enzyme (DUB) that plays a critical role in regulating the stability of several key proteins involved in cancer progression, including the E3 ligase **MDM2** and the tumor suppressor **p53**. By inhibiting USP7, TRIA-2 prevents the deubiquitination of MDM2, leading to its proteasomal degradation. The resulting decrease in MDM2 levels allows for the stabilization and accumulation of p53, which triggers cell cycle arrest and apoptosis in p53-wild-type tumor cells. Beyond the MDM2-p53 axis, TRIA-2 has demonstrated the ability to modulate other oncogenic drivers such as **N-Myc**, making it a promising candidate for a variety of solid tumors and hematologic malignancies. TRIA-2 is part of Triana's broader effort to leverage its molecular glue and DUB inhibition platform for targeted protein modulation in oncology.