Structure of malhamensilipin A, an inhibitor of protein tyrosine kinase, from the cultured chrysophyte Poterioochromonas malhamensis

J Nat Prod. 1994 Apr;57(4):524-7. doi: 10.1021/np50106a015.

Abstract

A new chlorosulfolipid, malhamensilpin A [1] was isolated from the cultured chrysophyte Poterioochromonas malhamensis. Malhamensilipin A was demonstrated to be a modest inhibitor of pp60v-src protein tyrosine kinase. The structure was determined by detailed spectral analysis to be a novel C24 hexachloro lipid containing a vinyl sulfate ester (2,11,12,13,15,16-hexachloro-14-hydroxy-n-tetracos-1E-enol-1-sulfa te).

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacteria / drug effects
  • Chromatography, Gel
  • Eukaryota / chemistry*
  • Lipids / chemistry
  • Lipids / isolation & purification*
  • Lipids / pharmacology
  • Magnetic Resonance Spectroscopy
  • Microbial Sensitivity Tests
  • Protein-Tyrosine Kinases / antagonists & inhibitors*

Substances

  • Lipids
  • malhamensilipin A
  • Protein-Tyrosine Kinases