Competitive Advantages
- Potent, specific, and cell permeable to target intracellular PPIs
- High stability against enzymatic degradation
- More effective than other peptides at antagonizing Wnt/β-catenin signaling
Summary
Protein-protein interactions (PPIs) are vital to the survival of cancer cells and are therefore a good target for anti-cancer therapeutics. Current therapies modulate protein allosteric sites as well as other prevalent protein interaction areas for drug- design strategies. A series of helical peptides has been developed that disrupt necessary PPIs in B-cell acute lymphoblastic leukemia cancer cells. The novel peptides, termed sulfono-γ-AA peptides, can structurally and functionally mimic the secondary structure of B-cell lymphoma 9 (BCL9) proteins. They selectively disrupt the PPIs between BCL9 proteins and β−catenin proteins, which are known to play an important role in the cellular adhesion and gene transcription of cancer cells. This technology is able to enter cancer cells and disrupt their PPIs at a much greater potency than other available peptides. The design of these helical sulfono-γ-AA peptides could lead to the development of a new modulation strategy regarding PPIs and anti-cancer therapeutics.
A-C) Crystal structure of sulfono-γ-AApeptide; (D) Binding of a sulfono-γ-AApeptide to β−catenin and disrupt BCL9/ β−catenin PPI
Desired Partnerships
- License
- Sponsored Research
- Co-Development