Apamin as a template for structure-based rational design of potent peptide activators of p53

Chong Li*, Marzena Pazgier, Min Liu, Wei Yue Lu, Wuyuan Lu

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

67 Scopus citations

Abstract

Taking the sting out of tumors: The oncoproteins MDM2 and MDMX negatively regulate the activity and stability of the tumor suppressor protein p53 and are important molecular targets for anticancer therapy. Grafting four residues critical for MDM2/MDMX binding to the C-terminal a-helix of apamin (see structure) converts the bee-venom neurotoxin into a novel class of potent p53 activators with potential antitumor activity.

Original languageEnglish
Pages (from-to)8712-8715
Number of pages4
JournalAngewandte Chemie - International Edition
Volume48
Issue number46
DOIs
StatePublished - 2 Nov 2009
Externally publishedYes

Keywords

  • Antitumor agents
  • P53
  • Protein structures
  • Protein-protein interactions

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