A tetramic acid derivative with protein tyrosine phosphatase 1B inhibitory activity and a new nortriterpene glycoside from the Indonesian marine sponge Petrosia sp.
A tetramic acid derivative with protein tyrosine phosphatase 1B inhibitory activity and a new nortriterpene glycoside from the Indonesian marine sponge Petrosia sp.
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DOI：
10.1016/j.bmcl.2016.12.077
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发表时间：
2017-02
影响因子：
2.7
通讯作者：
Wilmar Maarisit;H. Yamazaki;Syu-ichi Kanno;Ayako Tomizawa;H. Rotinsulu;D. Wewengkang;D. Sumilat;K. Ukai;M. M. Kapojos-M.;M. Namikoshi
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文献类型：
--
作者：
Wilmar Maarisit;H. Yamazaki;Syu-ichi Kanno;Ayako Tomizawa;H. Rotinsulu;D. Wewengkang;D. Sumilat;K. Ukai;M. M. Kapojos-M.;M. Namikoshi
在从海洋生物中寻找蛋白酪氨酸磷酸酶1B（PTP 1B）抑制剂的过程中，已知的特特拉姆酸衍生物melophlin C（1）作为活性成分与新的降三萜皂苷sarasinoside S（2）和三种同系物一起被分离：从印尼海绵Petrosia sp.中分离得到3个化合物：sarasinosides A1（3），I1（4），J（5）。化合物1抑制PTP 1B活性，IC_（50）值为14.6 μM，而化合物2 - 5在15.2-16.0 μM时无活性。这是第一个研究报告的tetramic酸衍生物对PTP 1B活性的抑制作用。
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 A1(3), I1(4), and J (5), from the Indonesian marine sponge Petrosia sp. The structure of2was elucidated on the basis of its spectroscopic data. Compound1inhibited PTP1B activity with an IC50value of 14.6 μM, while compounds2–5were not active at 15.2–16.0 μM. This is the first study to report the inhibitory effects of a tetramic acid derivative on PTP1B activity.