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Discovery of potent antagonists of the antiapoptotic protein XIAP for the treatment of cancer.
Oost, Thorsten K; Sun, Chaohong; Armstrong, Robert C; Al-Assaad, Ali-Samer; Betz, Stephen F; Deckwerth, Thomas L; Ding, Hong; Elmore, Steven W; Meadows, Robert P; Olejniczak, Edward T; Oleksijew, Andrew; Oltersdorf, Tilman; Rosenberg, Saul H; Shoemaker, Alexander R; Tomaselli, Kevin J; Zou, Hua; Fesik, Stephen W.
Afiliación
  • Oost TK; Cancer Research, Global Pharmaceutical Research and Development, Abbott Laboratories, 100 Abbott Park Road, Abbott Park, Illinois 60064, USA. thorsten.oost@abbott.com
J Med Chem ; 47(18): 4417-26, 2004 Aug 26.
Article en En | MEDLINE | ID: mdl-15317454
Inhibitor of apoptosis (IAP) proteins are overexpressed in many cancers and have been implicated in tumor growth, pathogenesis, and resistance to chemo- or radiotherapy. On the basis of the NMR structure of a SMAC peptide complexed with the BIR3 domain of X-linked IAP (XIAP), a novel series of XIAP antagonists was discovered. The most potent compounds in this series bind to the baculovirus IAP repeat 3 (BIR3) domain of XIAP with single-digit nanomolar affinity and promote cell death in several human cancer cell lines. In a MDA-MB-231 breast cancer mouse xenograft model, these XIAP antagonists inhibited the growth of tumors. Close structural analogues that showed only weak binding to the XIAP-BIR3 domain were inactive in the cellular assays and showed only marginal in vivo activity. Our results are consistent with a mechanism in which ligands for the BIR3 domain of XIAP induce apoptosis by freeing up caspases. The present study validates the BIR3 domain of XIAP as a target and supports the use of small molecule XIAP antagonists as a potential therapy for cancers that overexpress XIAP.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fragmentos de Péptidos / Proteínas / Proteínas Portadoras / Apoptosis / Proteínas Mitocondriales / Antineoplásicos Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: J Med Chem Asunto de la revista: QUIMICA Año: 2004 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fragmentos de Péptidos / Proteínas / Proteínas Portadoras / Apoptosis / Proteínas Mitocondriales / Antineoplásicos Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: J Med Chem Asunto de la revista: QUIMICA Año: 2004 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos