Investigating peptide sequence variations for 'double-click' stapled p53 peptides.
نویسندگان
چکیده
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.
منابع مشابه
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ورودعنوان ژورنال:
- Organic & biomolecular chemistry
دوره 12 24 شماره
صفحات -
تاریخ انتشار 2014