Tat-Beclin peptide

Tat-Beclin peptide (also known as Tat-Beclin 1 or Tat-BECN1) is a cell-permeable, synthetic peptide designed to potently and selectively induce autophagy. Developed by researchers at the University of Texas Southwestern Medical Center, the peptide is derived from the HIV-1 Nef-binding domain of the mammalian autophagy protein Beclin 1 (residues 267–284) fused to the HIV-1 Tat protein transduction domain via a diglycine linker. Mechanistically, Tat-Beclin peptide acts by binding to Golgi-associated plant pathogenesis-related protein 1 (GAPR-1/GLIPR2), a negative regulator of autophagy, thereby releasing Beclin 1 to form active Class III phosphatidylinositol 3-kinase (PI3K) complexes and initiate autophagosome formation. It has been widely investigated in preclinical research for its therapeutic potential in infectious diseases (such as West Nile virus, chikungunya, and HIV-1), neurodegenerative disorders, metabolic dysfunction-associated steatotic liver disease (MASLD), and certain cancers.

Other names

TB-1TB1TB 1TB-1 peptideTB1 peptideTB 1 peptideTat-BECN1Tat-BECN-1Tat-BECN 1Tat-Beclin 1Tat-Beclin1Tat-Beclin-1Tat-Beclin-1 peptideTat-Beclin1 peptideTat-Beclin 1 peptide