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JOURNAL ARTICLE
RESEARCH SUPPORT, NON-U.S. GOV'T
Investigating peptide sequence variations for 'double-click' stapled p53 peptides.
Organic & Biomolecular Chemistry 2014 June 29
Stapling peptides for inhibiting the p53/MDM2 interaction is a promising strategy for developing anti-cancer therapeutic leads. We evaluate double-click stapled peptides formed from p53-based diazidopeptides with different staple positions and azido amino acid side-chain lengths, determining the impact of these variations on MDM2 binding and cellular activity. We also demonstrate a K24R mutation, necessary for cellular activity in hydrocarbon-stapled p53 peptides, is not required for analogous 'double-click' peptides.
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