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Updated: Jun 25, 2026

Yeast As a Chassis for Developing Functional Assays to Study Human P53
Published on: August 4, 2019
A highly potent and cellularly active beta-peptidic inhibitor of the p53/hDM2 interaction
Martin Hintersteiner1, Thierry Kimmerlin, Geraldine Garavel
1The University of Edinburgh, Centre for Translational and Chemical Biology, UK.
Abstract:
New and improved: The incorporation of a 6-chlorotryptophan (6-Cl-Trp) into a beta-peptide (M)-3(14) helix leads to a high-affinity hDM2 inhibitor, as demonstrated by fluorescence fluctuation analysis at single molecule resolution. When conjugated to penetratin, the newly derived hDM2 binder specifically inhibits tumour cell growth in vitro.
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