Verticilide, a new ryanodine-binding inhibitor, produced by Verticillium sp. FKI-1033

J Antibiot (Tokyo). 2010 Feb;63(2):77-82. doi: 10.1038/ja.2009.126. Epub 2010 Jan 8.

Abstract

A new ryanodine-binding inhibitor, verticilide, was isolated from the cultured broth of a fungus, Verticillium sp. FKI-1033. It is a 24-membered ring cyclic depsipeptide, its structure being elucidated as cyclo[(2R)-2-hydroxyheptanoyl-N-methyl- L-alanyl](4). Verticilide inhibited ryanodine binding to ryanodine receptors in the cockroach at an IC(50) value of 4.2 microM, whereas inhibition against mouse ryanodine receptors was weak (IC(50)=53.9 microM).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Membrane / metabolism
  • Cockroaches
  • Depsipeptides / chemistry
  • Depsipeptides / metabolism*
  • Depsipeptides / pharmacology*
  • Mice
  • Molecular Biology
  • Muscle Fibers, Skeletal / metabolism
  • Protein Binding
  • Ryanodine / antagonists & inhibitors*
  • Ryanodine Receptor Calcium Release Channel / metabolism*
  • Structure-Activity Relationship
  • Verticillium / metabolism*

Substances

  • Depsipeptides
  • Ryanodine Receptor Calcium Release Channel
  • verticilide
  • Ryanodine