A novel sarsolenane diterpene, named secodihydrosarsolenone （1）, as a minor component was obtained from the South China Sea soft coral Sarcophyton trocheliophorum Marenzeller. Its structure was elucidated by detaile...A novel sarsolenane diterpene, named secodihydrosarsolenone （1）, as a minor component was obtained from the South China Sea soft coral Sarcophyton trocheliophorum Marenzeller. Its structure was elucidated by detailed spectroscopic analysis. Compound 1 exhibited moderate inhibitory activity （IC50= 13.7 μmol·L^-1） against protein tyrosine phosphatase 1B （PTP1B）, a key target for the treatment of type 2 diabetes, representing the first report of PTP1B inhibitory activity for sarsolenane diterpenes. This discovery promotes computational prediction of binding mode between the enzyme and the metabolite, suggesting a crucial role of the residues Tyr46, Ser216 and Arg221 in the binding action.展开更多
基金Acknowledgement This research work was financially supported by the National Natural Science Foundation of China （Nos. 41506187, 81520108028, 21672230, 41676073, 81603022）, SCTSM Project （No. 15431901000, 14431901100）, the Hunan Provincial Natural Science Foundation of China （2015JJ3176）, and the SKLDR/SIMM Projects （No. SIMMI501ZZ-03）. Linfu Liang thanks to the financial support of the China Postdoctoral Science Foundation （2016M601677）. The authors are grateful to Mr. Li-Gong Yao of State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, CAS, for his valuable work on collection of the sample.
文摘A novel sarsolenane diterpene, named secodihydrosarsolenone （1）, as a minor component was obtained from the South China Sea soft coral Sarcophyton trocheliophorum Marenzeller. Its structure was elucidated by detailed spectroscopic analysis. Compound 1 exhibited moderate inhibitory activity （IC50= 13.7 μmol·L^-1） against protein tyrosine phosphatase 1B （PTP1B）, a key target for the treatment of type 2 diabetes, representing the first report of PTP1B inhibitory activity for sarsolenane diterpenes. This discovery promotes computational prediction of binding mode between the enzyme and the metabolite, suggesting a crucial role of the residues Tyr46, Ser216 and Arg221 in the binding action.
