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Issue 24, 2014
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Investigating peptide sequence variations for ‘double-click’ stapled p53 peptides

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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 activity. We also demonstrate a K24R mutation, necessary for cellular activity in hydrocarbon-stapled p53 peptides, is not required for analogous ‘double-click’ peptides.

Graphical abstract: Investigating peptide sequence variations for ‘double-click’ stapled p53 peptides

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Publication details

The article was received on 08 Apr 2014, accepted on 01 May 2014 and first published on 02 May 2014


Article type: Communication
DOI: 10.1039/C4OB00742E
Citation: Org. Biomol. Chem., 2014,12, 4074-4077
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    Investigating peptide sequence variations for ‘double-click’ stapled p53 peptides

    Y. H. Lau, P. de Andrade, N. Sköld, G. J. McKenzie, A. R. Venkitaraman, C. Verma, D. P. Lane and D. R. Spring, Org. Biomol. Chem., 2014, 12, 4074
    DOI: 10.1039/C4OB00742E

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