PRIMA-1 reactivates mutant p53 by covalent binding to the core domain

Author: Lambert, Jeremy M. R.; Gorzov, Petr; Veprintsev, Dimitry B.; Soderqvist, Maja; Segerback, Dan; Bergman, Jan; Fersht, Alan R.; Hainaut, Pierre; Wiman, Klas G.; Bykov, Vladimir J. N.

Description: Restoration of wild-type p53 expression triggers cell death and eliminates tumors in vivo. The identification of mutant p53-reactivating small molecules such as PRIMA-1 opens possibilities for the development of more efficient anticancer drugs. Although the biological effects of PRIMA-1 are well demonstrated, little is known about its molecular mechanism of action. We show here that PRIMA-1 is converted to compounds that form adducts with thiols in mutant p53. Covalent modification of mutant p53 per se is sufficient to induce apoptosis in tumor cells. These findings might facilitate the design of more potent and specific mutant p53-targeting anticancer drugs.

Subject headings: Animals; Antineoplastic Agents; Apoptosis; Aza Compounds; Bridged Bicyclo Compounds; Heterocyclic; Cell Line; Tumor; Drug Design; Humans; Mice; Mutation; Neoplasms; Protein Binding; Protein Structure; Tertiary; Tumor Suppressor Protein p53

Publication year: 2009

Journal or book title: Cancer Cell

Volume: 15

Issue: 5

Pages: 376-388

Find the full text: https://www.strategian.com/fulltext/Lambert2009.pdf

Find more like this one (cited by): https://scholar.google.com/scholar?cites=197764644753845382&as_sdt=1000005&sciodt=0,16&hl=en

Serial number: 4015

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