1287745-42-9Relevant articles and documents
Β?CATENIN/ B-CELL LYMPHOMA 9 PROTEIN?PROTEIN INTERACTION INHIBITING PEPTIDOMIMETICS
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Paragraph 0167, (2020/11/03)
Disclosed herein is a series of helical sulfono-γ-AApeptides that mimic the binding mode of the α-helical HD2 domain of B-Cell Lymphoma 9 (BCL9). As disclosed herein, sulfono-γ-AApeptides can structurally and functionally mimic the α-helical domain of BCL9, and selectively disrupt β?catenin/BCL9 PPIs with even higher potency. More intriguingly, these sulfono-γ-AApeptides can enter cancer cells, bind with β?catenin and disrupt β?catenin/BCL PPI, and exhibit excellent cellular activity, which is much more potent than the BCL9 peptide. Furthermore, enzymatic stability studies demonstrated the remarkable stability of the helical sulfono-γ-AApeptides, with no degradation in the presence of pronase for 24 h, augmenting their biological potential.
γ-AApeptides: Design, synthesis and evaluation
Niu, Youhong,Hu, Yaogang,Li, Xiaolong,Chen, Jiandong,Cai, Jianfeng
, p. 542 - 545 (2011/06/20)
A new class of peptide mimics termed "γ-AApeptides" has been described. The design and synthesis of γ-AApeptides, and potential bioactivities towards p53/MDM2 interaction were demonstrated. γ-AApeptides were also found to be highly resistant to proteolysis. The development of sequence-specific γ-AApeptides may lead to a family of peptidomimetics with a new framework for drug discovery or peptide/protein mimicry.