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

doi:10.1002/anie.200904550

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 journal › Article › peer-review

69 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 language	English
Pages (from-to)	8712-8715
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	48
Issue number	46
DOIs	https://doi.org/10.1002/anie.200904550
State	Published - 2 Nov 2009
Externally published	Yes

Keywords

Antitumor agents
P53
Protein structures
Protein-protein interactions

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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.",

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AU - Liu, Min

AU - Lu, Wei Yue

AU - Lu, Wuyuan

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KW - Protein structures

KW - Protein-protein interactions

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

Abstract

Keywords

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