Kempopeptins A and B, serine protease inhibitors with different selectivity profiles from a marine cyanobacterium, Lyngbya sp.
Kempopeptins A and B, serine protease inhibitors with different selectivity profiles from a marine cyanobacterium, Lyngbya sp.
复制标题
DOI：
10.1021/np8002172
复制
发表时间：
2008-09-01
影响因子：
5.1
通讯作者：
Luesch, Hendrik
中科院分区：
文献类型：
--
作者：
Taori, Kanchan;Paul, Valerie J.;Luesch, Hendrik
从佛罗里达海洋蓝细菌Lyngbya sp.中分离到两种环缩肽，命名为kempopeptin A（1）和B（2），其先前提供了结构上相关的有效弹性蛋白酶抑制剂lyngbyastatin 7和somamide B。1和2的结构主要通过1D和2D NMR光谱进行了解析，并且通过手性HPLC和Marveland的降解产物分析确定了绝对构型。Kempopeptin A（1）对弹性蛋白酶的IC（50）为0.32 μ M，对胰凝乳蛋白酶的IC（50）为2.6 μ M，而Kempopeptin B（2）对胰蛋白酶的IC（50）为8.4 μ M。
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 IC(50) against elastase of 0.32 mu M and against chymotrypsin of 2.6 mu M, while kempopeptin B (2) inhibited trypsin with an IC(50) of 8.4 mu M.