Structure and Configuration of Phosphoeleganin, a Protein Tyrosine Phosphatase 1B Inhibitor from the Mediterranean Ascidian Sidnyum elegans

J Nat Prod. 2016 Apr 22;79(4):1144-8. doi: 10.1021/acs.jnatprod.6b00063. Epub 2016 Apr 11.

Abstract

A new phosphorylated polyketide, phosphoeleganin (1), has been isolated from the Mediterranean ascidian Sidnyum elegans. Its structure and configuration have been determined by extensive use of 2D NMR and microscale chemical degradation and/or derivatization. Phosphoeleganin (1) inhibited the protein tyrosine phosphatase 1B (PTP1B) activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Mediterranean Region
  • Molecular Structure
  • Nuclear Magnetic Resonance, Biomolecular
  • Polyketides / chemistry
  • Polyketides / isolation & purification*
  • Polyketides / pharmacology*
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1 / antagonists & inhibitors*
  • Urochordata / chemistry*

Substances

  • Polyketides
  • phosphoeleganin
  • PTPN1 protein, human
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1