Pompanopeptins A and B, new cyclic peptides from the marine cyanobacterium Lyngbya confervoides
Pompanopeptins A and B, new cyclic peptides from the marine cyanobacterium Lyngbya confervoides
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DOI：
10.1016/j.tet.2008.02.035
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发表时间：
2008-04-28
期刊：
影响因子：
2.1
通讯作者：
Luesch, Hendrik
中科院分区：
文献类型：
--
作者：
Matthew, Susan;Ross, Cliff;Luesch, Hendrik
从采自美国佛罗里达州东南海岸的海洋蓝藻中分离得到一个新的含肽内酯的3-氨基-6-羟基-2-哌酮(AHP)，pompanopeptin A(1)和一个新的N-甲基-2-氨基-6-(4‘-羟基苯基)己酸(N-me-Ahpha)，其中环五肽与第六个氨基酸残基通过一个罕见的缩脲键相连，pompanopeptin B(2)。通过核磁共振光谱分析和质谱分析相结合的方法确定了它们的平面结构。利用改进的Marfey方法和化学降解产物的手性高效液相分析建立了绝对构型。化合物1选择性地抑制胰酶而不是弹性酶和胰凝乳酶，其IC(50)值为2.4微米；选择性是由环核中的精氨酸残基赋予的。(C)2008爱思唯尔有限公司。保留所有权利。
A new 3-amino-6-hydroxy-2-piperidone (Ahp) containing peptolide, pompanopeptin A (1), and a novel N-methyl-2-amino-6-(4'-hydroxyphenyl)hexanoic acid (N-Me-Ahpha) containing cyclic pentapeptide connected with a sixth amino acid residue via a rare ureido linkage, pompanopeptin B (2), were isolated from the marine cyanobacterium Lyngbya confervoides collected from the southeastern coast of Florida. Their planar structures were determined by a combination of NMR spectroscopic analysis and mass spectrometry. The absolute configurations were established using advanced Marfey's method and chiral HPLC analysis of the chemical degradation products. Compound 1 selectively inhibited trypsin over elastase and chymotrypsin, with an IC(50) value of 2.4 mu M; selectivity is conferred by an arginine residue in the cyclic core. (c) 2008 Elsevier Ltd. All rights reserved.