Cover Picture: Chemistry and Biology of the Aeruginosin Family of Serine Protease Inhibitors (Angew. Chem. Int. Ed. 7/2008)

Authors

  • Karolina Ersmark Dr.,

    1. Department of Chemistry, Université de Montréal, C.P. 6128, Station Centre-ville, Montréal, PQ, H3C 3J7, Canada, Fax: (+1) 514-343-5728
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  • Juan R. Del Valle Dr.,

    1. Department of Chemistry and Biochemistry, New Mexico State University, 1175 North Horseshoe Drive MSC 3C, Las Cruces, NM 88003, USA
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  • Stephen Hanessian Prof.

    1. Department of Chemistry, Université de Montréal, C.P. 6128, Station Centre-ville, Montréal, PQ, H3C 3J7, Canada, Fax: (+1) 514-343-5728
    2. Department of Chemistry, University of Caifornia, Irvine, 516 Rowland Hall, Irvine, CA 92697-2025, USA
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Abstract

original image

Different phyla and different oceans are sources of linear peptides in the aeruginosin family which comprise a central hydroxy- (or dihydroxy-) octahydroindole carboxamide core unit onto which unusual amino acids are appended. The aeruginosins exhibit varying degrees of inhibitory activity against serine proteases, including factor II (thrombin) and factor VIIa of the blood coagulation cascade. In their Review on page 1202 ff., S. Hanessian et al. provide an overview of the chemical and biological properties of the aeruginosins as well as the natural sources of these compounds, their total syntheses, and structure revisions.

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