Investigating peptide sequence variations for 'double-click' stapled p53 peptides.

Abstract

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… (More)
DOI: 10.1039/c4ob00742e

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@article{Lau2014InvestigatingPS, title={Investigating peptide sequence variations for 'double-click' stapled p53 peptides.}, author={Yu Heng Lau and Peterson de Andrade and Niklas Sk{\"o}ld and Grahame J. McKenzie and Ashok R. Venkitaraman and Chandra Verma and David Philip Lane and David R. Spring}, journal={Organic & biomolecular chemistry}, year={2014}, volume={12 24}, pages={4074-7} }