Issue 24, 2014

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 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

Supplementary files

Article information

Article type
Communication
Submitted
08 Apr 2014
Accepted
01 May 2014
First published
02 May 2014

Org. Biomol. Chem., 2014,12, 4074-4077

Author version available

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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