Three New Pigment Protein Tyrosine Phosphatases Inhibitors from the Insect Parasite Fungus Cordyceps gracilioides: Terreusinone A, Pinophilin C and Cryptosporioptide A
Pei-Yao Wei,
Lin-Xia Liu,
Ting Liu,
Chuan Chen,
Du-Qiang Luo,
Bao-Zhong Shi
Affiliations
Pei-Yao Wei
College of Life Science, Key Laboratory of Medicinal Chemistry and Molecular Diagnosis of Ministry of Education, Hebei University, Baoding 071002, China
Lin-Xia Liu
College of Life Science, Key Laboratory of Medicinal Chemistry and Molecular Diagnosis of Ministry of Education, Hebei University, Baoding 071002, China
Ting Liu
College of Life Science, Key Laboratory of Medicinal Chemistry and Molecular Diagnosis of Ministry of Education, Hebei University, Baoding 071002, China
Chuan Chen
College of Life Science, Key Laboratory of Medicinal Chemistry and Molecular Diagnosis of Ministry of Education, Hebei University, Baoding 071002, China
Du-Qiang Luo
College of Life Science, Key Laboratory of Medicinal Chemistry and Molecular Diagnosis of Ministry of Education, Hebei University, Baoding 071002, China
Bao-Zhong Shi
Biotechnology Center of Hebei Province, Hebei University, Baoding 071002, China
Three new pigment compounds—terreusinone A (1), pinophilin C (2) and cryptosporioptide A (3)—were isolated from a solid culture of Cordyceps gracilioides. The structures of these compounds were determined by extensive spectroscopic analysis including HRESIMS, 1D- and 2D-NMR. The structure of terreusinone A (1) was further confirmed by single-crystal X-ray crystallographic diffraction analysis. In an in vitro activity assay, 1, 2 and 3 exhibited high inhibitory activity against PTP1B, SHP2, CDC25B, LAR and SHP1. Terreusinone A (1) inhibited PTP1B, SHP2, CDC25B, LAR and SHP1 enzyme with IC50 values 12.5, >50, 4.1, 10.6, 5.6 µg/mL, respectively; pinophilin C (2) with IC50 values 6.8, 8.0, 4.5, 4.7, 3.4 µg/mL, respectively; and cryptosporioptide A (3) with IC50 values 7.3, 5.7, 7.6, >50, 4.9 µg/mL, respectively.
