7w36

Publication Abstract from PubMed

Selective modulation of autophagy is a promising therapeutic strategy, especially for cancer treatment. However, the lack of specific autophagy inhibitors limits this strategy. The formation of the ATG12-ATG5-ATG16L1 complex is essential for targeting the ATG12-ATG5 conjugate to proper membranes and to generate LC3-II for the progression of autophagy. Thus, targeting ATG5-ATG16L1 protein-protein interactions (PPIs) might inhibit early stage autophagy with high specificity. In this paper, we report that a stapled peptide derived from ATG16L1 exhibits potent binding affinity to ATG5, striking resistance to proteolysis, and significant autophagy inhibition activities in cells.

Targeting the ATG5-ATG16L1 Protein-Protein Interaction with a Hydrocarbon-Stapled Peptide Derived from ATG16L1 for Autophagy Inhibition.,Cui J, Ogasawara Y, Kurata I, Matoba K, Fujioka Y, Noda NN, Shibasaki M, Watanabe T J Am Chem Soc. 2022 Sep 28;144(38):17671-17679. doi: 10.1021/jacs.2c07648. Epub , 2022 Sep 15. PMID:36107218^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.