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  • Title: Kempopeptins A and B, serine protease inhibitors with different selectivity profiles from a marine cyanobacterium, Lyngbya sp.
    Author: Taori K, Paul VJ, Luesch H.
    Journal: J Nat Prod; 2008 Sep; 71(9):1625-9. PubMed ID: 18693761.
    Abstract:
    Two cyclodepsipeptides named kempopeptins A (1) and B (2) were isolated from a collection of a Floridian marine cyanobacterium, Lyngbya sp., that had previously afforded the structurally related potent elastase inhibitors lyngbyastatin 7 and somamide B. The structures of 1 and 2 were elucidated mainly by 1D and 2D NMR spectroscopy, and the absolute configuration was established by chiral HPLC and Marfey's analysis of the degradation products. Kempopeptin A (1) exhibited an IC50 against elastase of 0.32 microM and against chymotrypsin of 2.6 microM, while kempopeptin B (2) inhibited trypsin with an IC50 of 8.4 microM.
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