Clavatadine A, A Natural Product with Selective Recognition and Irreversible Inhibition of Factor XIa
Journal of Medicinal Chemistry2008Vol. 51(12), pp. 3583–3587
Citations Over TimeTop 11% of 2008 papers
Malcolm S. Buchanan, Anthony R. Carroll, Deborah Wessling, Michael F. Jobling, Vicky M. Avery, Rohan A. Davis, Yunjiang Feng, Yafeng Xue, Linda Öster, Tomas Fex, Johanna Deinum, John N. A. Hooper, Ronald J. Quinn
Abstract
Bioassay-guided fractionation of a CH2Cl2/MeOH extract of the sponge Suberea clavata using the serine protease factor XIa to detect antithrombotic activity led to the isolation of the new marine natural products, clavatadines A and B. Clavatadines A and B inhibited factor XIa with IC50's of 1.3 and 27 microM, respectively. A crystal structure of protein-inhibitor (clavatadine A) complex was obtained and revealed interesting selective binding and irreversible inhibition of factor XIa. The cocrystal structure provides guidance for the design and synthesis of future factor XIa inhibitors as antithrombotic agents.
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