Raymond and Beverly Sackler School of Chemistry and Faculty of Exact Sciences, Tel-Aviv University, Ramat Aviv, Tel-Aviv 69978, Israel.
Mar Drugs. 2017 Dec 1;15(12):371. doi: 10.3390/md15120371.
Two new natural products, micropeptin TR1058 () and aeruginosin TR642 (), were isolated from the hydrophilic extract of bloom material of sp. collected from the Timurim water reservoir in Israel. The structures of compounds and were determined using 1D and 2D NMR spectroscopy and HR ESI MS and MS/MS techniques. Micropeptin TR1058 () was extremely unstable under the isolation conditions, and several degradation products were identified. NMR analysis of aeruginosin TR642 () revealed a mixture of eight isomers, and elucidation of its structure was challenging. Aeruginosin TR642 contains a 4,5-didehydroaraginal subunit that has not been described before. Micropeptin TR1058 () inhibited chymotrypsin with an IC of 6.78 µM, and aeruginosin TR642 () inhibited trypsin and thrombin with inhibition concentration (IC) values of 3.80 and 0.85 µM, respectively. The structures and biological activities of the new compounds are discussed.
从以色列提姆林水库中采集的 sp. 的水华材料的亲水性提取物中分离得到两个新的天然产物，微缩肽 TR1058 () 和绿蝇菌素 TR642 ()。通过 1D 和 2D NMR 光谱以及高分辨 ESI MS 和 MS/MS 技术确定了化合物 和 的结构。微缩肽 TR1058 () 在分离条件下极不稳定，鉴定出了几种降解产物。绿蝇菌素 TR642 () 的 NMR 分析显示存在八种异构体的混合物，其结构阐明具有挑战性。绿蝇菌素 TR642 含有一个以前未描述过的 4,5-二脱氢阿拉基宁亚基。微缩肽 TR1058 () 对胰凝乳蛋白酶的抑制作用的 IC 为 6.78 µM，而绿蝇菌素 TR642 () 对胰蛋白酶和凝血酶的抑制浓度 (IC) 值分别为 3.80 和 0.85 µM。讨论了新化合物的结构和生物活性。
