Structural analysis of bengamide derivatives as inhibitors of methionine aminopeptidases

Wei Xu, Jing Ping Lu, Qi Zhuang Ye

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


Natural-product-derived bengamides possess potent antiproliferative activity and target human methionine aminopeptidases (MetAPs) for their cellular effects. Several derivatives were designed, synthesized, and evaluated as MetAP inhibitors. Here, we present four new X-ray structures of human MetAP1 in complex with the inhibitors. Together with the previous structures of bengamide derivatives with human MetAP2 and tubercular MtMetAP1c, analysis of the interactions of these inhibitors at the active site provides structural basis for further modification of these bengamide inhibitors for improved potency and selectivity as anticancer and antibacterial therapeutics.

Original languageEnglish (US)
Pages (from-to)8021-8027
Number of pages7
JournalJournal of Medicinal Chemistry
Issue number18
StatePublished - Sep 27 2012

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery

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