sulfopin

**Sulfopin** is a potent, selective, covalent small molecule inhibitor of the enzyme **peptidyl-prolyl isomerase NIMA-interacting 1 (Pin1)**. It acts by covalently binding to the active site cysteine (Cys113) of Pin1, with nanomolar potency (Ki = 17 nM). Sulfopin blocks the function of Pin1, an enzyme that controls phosphorylation-dependent proline isomerization, impacting protein stability, activity, subcellular localization, and interactions relevant to diverse signaling pathways. Pin1 has been implicated in cancer for activating oncogenes (e.g., MYC) and inactivating tumor suppressors. Sulfopin downregulates MYC target gene expression, reduces tumor progression, and extends survival in MYCN-driven neuroblastoma and pancreatic cancer animal models. The compound demonstrates high selectivity for Pin1, minimal toxicity in preclinical studies, and is suitable for oral administration. Developed as a research probe, Sulfopin is used to explore Pin1-dependent pharmacology in vitro and in vivo[1][2][3][4].