Design Peptide for E3 ubiquitin ligase

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As a leading service provider in drug discovery and development, BOC Sciences is fully qualified and committed to providing one-stop PROTAC® development services, which has become a promising strategy in the field of small molecular drug discovery. With a comprehensive and advanced platform, we provide peptide Ligand Design for E3 Ligase to customers around the world to meet new drug discovery goals.


The Ubiquitin-proteasome system (UPS) is the main signal pathway to regulate intracellular protein levels. E3 ubiquitin ligase is a substrate-specific member of UPS and represents an attractive protein target for drug development. E3 ligases are becoming increasingly important as expected targets for small molecule regulation, proving their role in cancer and other diseases. So far, the number of effective compounds targeting E3 ligase is still very small, and its reasonable design constitutes a challenging task. Related studies reported the design of phosphorylated peptide Protacs. The researchers designed two phosphorylated peptides Protacs, to couple the tyrosine phosphorylation sequence of nerve growth factor receptor TrkA (tropomyosin receptor kinase A) or neuromodulin receptor ErbB3 (polycythemia oncogene B3) with the peptide ligand of E3 ubiquitin ligase Von Hippel Lindau. These two phosphorylated peptides Protacs peptides recruit fibroblast growth factor receptor substrate 2 α or survival-promoting phosphatidylinositol-3 kinase, which are neurotrophic signal effectors, respectively, and are ubiquitinated and degraded by E3 ubiquitin ligase VHL. The researchers demonstrated the ability of these two phosphorylated peptides Protacs to inhibit the short-term and long-term effects of their respective activated receptor tyrosine kinase pathways in vitro and in vivo.


Phosphorylated peptide Protacs preferentially degrades PI3K, in cells with high levels of ErbB2/ErbB3 signal transduction and preferentially inhibits the proliferation of breast or ovarian or pancreatic cancer cells. Another advantage of using phosphorylated peptide Protacs is that it is less likely to cause drug resistance mutations. Phosphorylatedpeptide Protacs can degrade target proteins of different signal transduction pathways, because many important tyrosine kinases, such as proteins containing SH2 or PTB domains, are known to bind to each other, and it will lead the way in the field of drug design of target proteins in "unfinished drugs".

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Workflow of Ligand Design Services

Design Peptide for E3 ubiquitin ligase


  1. Rees, I., Lee, S., Kim, H., & Tsai, F. T. (2006). The E3 ubiquitin ligase CHIP binds the androgen receptor in a phosphorylation-dependent manner. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1764(6), 1073-1079.
  2. McDermott, J. E., Cort, J. R., Nakayasu, E. S., Pruneda, J. N., Overall, C., & Adkins, J. N. (2019). Prediction of bacterial E3 ubiquitin ligase effectors using reduced amino acid peptide fingerprinting. PeerJ, 7, e7055.

* PROTAC® is a registered trademark of Arvinas Operations, Inc., and is used under license.

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