期刊
ORGANIC & BIOMOLECULAR CHEMISTRY
卷 12, 期 24, 页码 4074-4077出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c4ob00742e
关键词
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资金
- Agency for Science, Technology and Research
- European Union
- Engineering and Physical Sciences Research Council
- Biotechnology and Biological Sciences Research Council
- Medical Research Council
- Wellcome Trust
- Cambridge Trusts
- Engineering and Physical Sciences Research Council [EP/J016012/1] Funding Source: researchfish
- Medical Research Council [MC_UU_12022/1, MC_UU_12022/8, MC_U105359877, G1001521, G1001522] Funding Source: researchfish
- EPSRC [EP/J016012/1] Funding Source: UKRI
- MRC [G1001522, MC_UU_12022/1, MC_U105359877, G1001521, MC_UU_12022/8] Funding Source: UKRI
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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