一种具有蛋白酪氨酸磷酸酶1B抑制活性的四咪酸衍生物以及从印度尼西亚海洋海绵Petrosia sp.中分离得到的一种新的降三萜糖苷。
A tetramic acid derivative with protein tyrosine phosphatase 1B inhibitory activity and a new nortriterpene glycoside from the Indonesian marine sponge Petrosia sp.
作者信息
Maarisit Wilmar, Yamazaki Hiroyuki, Kanno Syu-Ichi, Tomizawa Ayako, Rotinsulu Henki, Wewengkang Defny S, Sumilat Deiske A, Ukai Kazuyo, Kapojos Magie M, Namikoshi Michio
机构信息
Faculty of Pharmaceutical Sciences, Tohoku Medical and Pharmaceutical University, Sendai 981-8558, Japan; Faculty of Fisheries and Marine Science, Sam Ratulangi University, Kampus Bahu, Manado 95115, Indonesia.
Faculty of Pharmaceutical Sciences, Tohoku Medical and Pharmaceutical University, Sendai 981-8558, Japan.
出版信息
Bioorg Med Chem Lett. 2017 Feb 15;27(4):999-1002. doi: 10.1016/j.bmcl.2016.12.077. Epub 2016 Dec 31.
During the search for protein tyrosine phosphatase 1B (PTP1B) inhibitors from marine organisms, the known tetramic acid derivative, melophlin C (1), was isolated as an active component together with the new nortriterpenoid saponin, sarasinoside S (2), and three homologues: sarasinosides A (3), I (4), and J (5), from the Indonesian marine sponge Petrosia sp. The structure of 2 was elucidated on the basis of its spectroscopic data. Compound 1 inhibited PTP1B activity with an IC value of 14.6μM, while compounds 2-5 were not active at 15.2-16.0μM. This is the first study to report the inhibitory effects of a tetramic acid derivative on PTP1B activity.
在从海洋生物中寻找蛋白酪氨酸磷酸酶1B（PTP1B）抑制剂的过程中，从印度尼西亚海洋海绵Petrosia sp.中分离出了已知的四胺酸衍生物美洛啡林C（1）作为活性成分，同时还分离出了新的降三萜皂苷萨拉西诺苷S（2）及其三个同系物：萨拉西诺苷A（3）、I（4）和J（5）。根据其光谱数据阐明了化合物2的结构。化合物1对PTP1B活性的抑制IC值为14.6μM，而化合物2 - 5在15.2 - 16.0μM时无活性。这是首次报道四胺酸衍生物对PTP1B活性的抑制作用的研究。
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