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

Content Provider	Semantic Scholar
Author	Lau, Yu Heng Andrade, Peterson De Sköld, Niklas McKenzie, Grahame J. Venkitaraman, Ashok R. Verma, Chandra Shekhar Lane, David Philip Spring, David R.
Copyright Year	2014
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.
File Format	PDF HTM / HTML
DOI	10.1039/c4ob00742e
PubMed reference number	24817343
Journal	Medline
Volume Number	12
Issue Number	24
Alternate Webpage(s)	http://www-spring.ch.cam.ac.uk/publications/pdf/2014_OBC_4074.pdf
Alternate Webpage(s)	https://doi.org/10.1039/c4ob00742e
Journal	Organic & biomolecular chemistry
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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