Tat-Beclin 1 L11 Autophagy Inducing Peptide

Unconjugated

Functional Assay

Cell-penetrating autophagy inducing peptides engineered in 2013 were demonstrated to induce autophagy through interaction with the autophagy suppressor GAPR-1/GLIPR2 (Nature, 2013; PMID 23364696). These Tat-Beclin 1 peptides were comprised of AA 267-284 of the autophagy inducer Beclin 1 (18 amino acids), a diglycine linker, and 11 amino acids of the HIV Tat protein transduction domain. Tat-Beclin 1 peptides were re-engineered to remove 7 AA from the beclin 1 domain. These shorter peptides, Tat-D11 [NBP2-49888] and Tat-L11 [NBP2-49886], demonstrate enhanced autophagy inducing function over the original Tat-Beclin 1 peptides and the scrambled control peptide Tat-L11S [NBP2-49887]. Tat-D11 and Tat-L11 are potent autophagy inducers which function both in vitro and in vivo to specifically induce autophagy. Tat-D11 and Tat-L11 peptides are comprised of 11 amino acids of the autophagy-inducing region of beclin 1 fused to the HIV Tat protein. Both Tat-D11 and Tat-L11 peptides function by binding the negative regulator of autophagy GAPR-1/GLIPR2. Upon peptide binding, beclin 1 bound to GARP-1 is released, resulting in beclin 1 mediated autophagosome formation and autophagy induction. Data indicate Tat-D11 is more potent than both Tat-L11 and Tat-Beclin 1 in vivo. In addition, initial data derived from HeLa cells also suggests Tat-D11 is more potent than Tat-L11 in vitro. However, ongoing experiments indicate Tat-L11 may be more potent than Tat-D11 in select cell lines.

3.08 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Autophagy Inducing Peptide