Absolute structure of prunustatin A, a novel GRP78 molecular chaperone down-regulator

Org Lett. 2007 Oct 11;9(21):4239-42. doi: 10.1021/ol7017856. Epub 2007 Sep 21.

Abstract

In the course of our screening program for regulators of a molecular chaperone GRP78 expression, we isolated a novel inhibitor of GRP78 expression, designated as prunustatin A, from Streptomyces violaceoniger 4521-SVS3. The planar structure of prunustatin A was determined to be an oxidized type of the neoantimycin family. Its absolute stereochemistry was established to be 2R, 4S, 6S, 7R, 9S, and 29S by analyzing chemically degraded components obtained from the derivative of prunustatin A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Endoplasmic Reticulum Chaperone BiP
  • Glucose / metabolism
  • Heat-Shock Proteins / drug effects*
  • Heat-Shock Proteins / metabolism
  • Humans
  • Macrolides / chemistry*
  • Macrolides / pharmacology*
  • Molecular Chaperones / drug effects*
  • Molecular Chaperones / metabolism
  • Molecular Structure
  • Organic Chemicals / chemistry
  • Peptides, Cyclic / chemistry
  • Stereoisomerism
  • Streptomyces / chemistry*
  • Tumor Cells, Cultured

Substances

  • Endoplasmic Reticulum Chaperone BiP
  • HSPA5 protein, human
  • Heat-Shock Proteins
  • Macrolides
  • Molecular Chaperones
  • Organic Chemicals
  • Peptides, Cyclic
  • SW-163A
  • prunustatin A
  • neoantimycin
  • Glucose