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Discovery Of Selective Small-molecule Inhibitors Of Key Protein-protein Interactions In The Wnt/?-catenin Signaling Pathway | 3785
ISSN: 0974-276X

Journal of Proteomics & Bioinformatics
Open Access

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Discovery of selective small-molecule inhibitors of key protein-protein interactions in the Wnt/?-catenin signaling pathway

2nd International Conference on Proteomics & Bioinformatics

Haitao (Mark) Ji

Accepted Abstracts: J Proteomics Bioinform

DOI: 10.4172/0974-276X.S1.065

The aberrant formation of the β-catenin/Tcf (T-cell factor) protein-protein complex in the canonical Wnt/β-catenin signaling cascades has been recognized as the major driving force for human tumorigenesis and organ fibroses. Crystallographic analyses, however, reveal that the binding modes of Tcf, cadherin (essential for the cell-cell adhesion) and APC (adenomatous polyposis coli, important for β-catenin degradation) with β-catenin are identical. Therefore, the design and synthesis of smallmolecule inhibitors to selectively disrupt β-catenin/Tcf protein-protein interactions while leaving β-catenin/Ecadherin and β-catenin/APC interactions untouched is critical but challenging. We are developing an innovative strategy to design smallmolecule inhibitors targeting to a specific protein-protein interface, and discovered three series of new small-molecule inhibitors for β-catenin/Tcf protein-protein interactions. Two of them are more potent than all existing β-catenin/Tcf inhibitors, and exhibit good cell-based activity to human colorectal cancer cell line and selectivity over normal cells.
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