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Apamin as a Template for Structure‐Based Rational Design of Potent Peptide Activators of p53
Author(s) -
Li Chong,
Pazgier Marzena,
Liu Min,
Lu WeiYue,
Lu Wuyuan
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200904550
Subject(s) - mdmx , peptide , computational biology , mdm2 , chemistry , apamin , cancer research , biochemistry , biology , gene , organic chemistry , calcium
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 α‐helix of apamin (see structure) converts the bee‐venom neurotoxin into a novel class of potent p53 activators with potential antitumor activity.