Three new pigment protein tyrosine phosphatases inhibitors from the insect parasite fungus Cordyceps gracilioides: terreusinone A, pinophilin C and cryptosporioptide A

Molecules. 2015 Apr 2;20(4):5825-34. doi: 10.3390/molecules20045825.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acrylates / chemistry
  • Acrylates / isolation & purification
  • Acrylates / pharmacology
  • Animals
  • Coleoptera / microbiology*
  • Cordyceps / chemistry*
  • Crystallography, X-Ray
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / isolation & purification
  • Enzyme Inhibitors / pharmacology*
  • Molecular Structure
  • Pigments, Biological / chemistry
  • Pigments, Biological / isolation & purification*
  • Pigments, Biological / pharmacology
  • Polyketides / chemistry
  • Polyketides / isolation & purification*
  • Polyketides / pharmacology
  • Protein Tyrosine Phosphatases / antagonists & inhibitors*

Substances

  • Acrylates
  • Enzyme Inhibitors
  • Pigments, Biological
  • Polyketides
  • cryptosporioptide A
  • pinophilin C
  • terreusinone A
  • Protein Tyrosine Phosphatases
  • acrylic acid