A left-handed solution to peptide inhibition of the p53-MDM2 interaction

Min Liu; Marzena Pazgier; Changqing Li; Weirong Yuan; Chong Li; Wuyuan Lu

doi:10.1002/anie.201000329

A left-handed solution to peptide inhibition of the p53-MDM2 interaction

Min Liu^*, Marzena Pazgier, Changqing Li, Weirong Yuan, Chong Li, Wuyuan Lu

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

98 Scopus citations

Abstract

Throwing tumors a left-hook punch: The oncoprotein MDM2 negatively regulates the activity and stability of the tumor suppressor protein p53, and is an important molecular target for anticancer therapy. Mirror-image phage display identified a high-affinity D-peptide ligand of MDM2 (see structure) that could be developed into a potent and protease-resistant p53 activator with potential antitumor activity. (Figure Presented)

Original language	English
Pages (from-to)	3649-3652
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	49
Issue number	21
DOIs	https://doi.org/10.1002/anie.201000329
State	Published - 10 May 2010
Externally published	Yes

Keywords

Antitumor agents
MDM2
P53
Protein structures
Protein-protein interactions

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10.1002/anie.201000329

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abstract = "Throwing tumors a left-hook punch: The oncoprotein MDM2 negatively regulates the activity and stability of the tumor suppressor protein p53, and is an important molecular target for anticancer therapy. Mirror-image phage display identified a high-affinity D-peptide ligand of MDM2 (see structure) that could be developed into a potent and protease-resistant p53 activator with potential antitumor activity. (Figure Presented)",

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AU - Pazgier, Marzena

AU - Li, Changqing

AU - Yuan, Weirong

AU - Li, Chong

AU - Lu, Wuyuan

PY - 2010/5/10

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KW - Antitumor agents

KW - MDM2

KW - P53

KW - Protein structures

KW - Protein-protein interactions

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A left-handed solution to peptide inhibition of the p53-MDM2 interaction

Abstract

Keywords

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