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A highly potent and cellularly active beta-peptidic inhibitor of the p53/hDM2 interaction.
Chembiochem : a European Journal of Chemical Biology 2009 April 18
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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