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Chemistry and biology of wortmannin

Wipf, P and Halter, RJ (2005) Chemistry and biology of wortmannin. Organic and Biomolecular Chemistry, 3 (11). 2053 - 2061. ISSN 1477-0520

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Abstract

Recent synthetic and biological studies of the viridin class of steroidal furans have revealed multiple opportunities for fundamental discoveries as well as advanced drug design. Wortmannin is a potent enzyme inhibitor that binds to the ATP site of important regulatory kinases such as PI-3 kinase and Polo-like kinase. The natural product shares a unique mechanism-based biological activation pathway with other viridins. Furthermore, while there have been several encouraging approaches toward the total synthesis of these compounds, there is still ample room for improvements in synthetic strategies and tactics, and the development of structurally simplified analogs that exert more specific biological effects and are devoid of toxicity issues that have thwarted the clinical development of the parent compounds. © The Royal Society of Chemistry 2005.

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Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Wipf, Ppwipf@pitt.eduPWIPF
Halter, RJ
Date: 7 June 2005
Date Type: Publication
Journal or Publication Title: Organic and Biomolecular Chemistry
Volume: 3
Number: 11
Page Range: 2053 - 2061
DOI or Unique Handle: 10.1039/b504418a
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 1477-0520
MeSH Headings: Adenosine Triphosphate--metabolism; Androstadienes--chemistry; Androstadienes--metabolism; Enzyme Inhibitors--chemistry; Enzyme Inhibitors--metabolism; Models, Molecular; Phosphatidylinositol 3-Kinases--antagonists & inhibitors; Phosphatidylinositol 3-Kinases--chemistry; Phosphatidylinositol 3-Kinases--metabolism
PubMed ID: 15917886
Date Deposited: 12 Nov 2013 17:17
Last Modified: 02 Feb 2019 15:56
URI: http://d-scholarship-dev.library.pitt.edu/id/eprint/19978

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