Tat-beclin 1

**Tat-beclin 1** is a synthetic cell-permeable peptide designed to induce autophagy. It consists of the HIV-1 Tat protein transduction domain linked via a diglycine linker to amino acids 267-284 of human beclin 1, a key autophagy regulator. The peptide binds and inhibits GAPR-1 (GLIPR2), a negative regulator of autophagy, thereby releasing beclin 1 to promote autophagosome formation and enhance autophagic flux. Originally developed by Beth Levine's group at UT Southwestern Medical Center, it demonstrates efficacy in preclinical models by reducing protein aggregates in polyglutamine disorders (e.g., Huntington's disease models), inhibiting replication of pathogens like HIV-1, Sindbis virus, chikungunya virus, West Nile virus, and Listeria monocytogenes, and improving outcomes in viral infection mouse models. It is commercially available as a research tool from suppliers like MedChemExpress, Sigma-Aldrich, and Cayman Chemical, with applications explored in neurodegeneration, infection, cancer (e.g., HER2+ breast cancer xenografts), and memory enhancement via mitophagy.

Other names

Tat-Beclin-1Tat-Beclin1Tat-Beclin 1T-B