ST1-Hel2A-2

ST1-Hel2A-2 (also referred to as ST1-H2A2) is a cell-permeable peptide inhibitor designed to selectively target the N-terminal domain of Signal Transducer and Activator of Transcription 1 (STAT1). Developed by researchers at the National Cancer Institute and Georgetown University, the peptide is derived from the second alpha-helix of the STAT1 N-domain and is fused to a penetratin sequence to facilitate intracellular delivery. ST1-Hel2A-2 selectively binds to STAT1, preventing its homodimerization and subsequent transcriptional activity without affecting other STAT family members. In preclinical studies, ST1-Hel2A-2 has been shown to sensitize breast cancer cells to ionizing radiation and chemotherapy by downregulating pro-survival genes (such as Hsp27 and Mcl-1) and disrupting STAT1 interactions with double-stranded RNA-activated protein kinase (PKR) and DNA glycosylase NEIL1, thereby impairing DNA repair mechanisms.

Other names

ST1-H2A2 peptideST-1-H2A2 peptideST 1-H2A2 peptideST1-Hel2A-2 peptideST-1-Hel2A-2 peptideST 1-Hel2A-2 peptide