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

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

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 imp...

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Bibliographic Details
Main Authors: Lau, Yu Heng, de Andrade, Peterson, Sköld, Niklas, McKenzie, Grahame J., Venkitaraman, Ashok R., Verma, Chandra, Lane, David P., Spring, David R.
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2016
Subjects:
Amino acids
Peptide sequences
Online Access:https://hdl.handle.net/10356/83841
http://hdl.handle.net/10220/41497
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Institution: Nanyang Technological University
Language: English
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Summary: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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