Rhizolutin, a Novel 7/10/6-Tricyclic Dilactone, Dissociates Misfolded Protein Aggregates and Reduces Apoptosis/Inflammation Associated with Alzheimer's Disease

Angew Chem Int Ed Engl. 2020 Dec 14;59(51):22994-22998. doi: 10.1002/anie.202009294. Epub 2020 Oct 4.

Abstract

Rhizolutin (1) was discovered as a natural product of ginseng-rhizospheric Streptomyces sp. WON17. Its structure features an unprecedented 7/10/6-tricyclic dilactone carbon skeleton composed of dimethylcyclodecatriene flanked by a 7-membered and a 6-membered lactone ring based on spectroscopic analysis. During an unbiased screening of natural product libraries, this novel compound was found to dissociate amyloid-β (Aβ) plaques and tau tangles, which are key pathological hallmarks of Alzheimer's disease (AD). Rhizolutin treatment of APP/PS1 double transgenic mice with AD significantly dissociated hippocampal plaques. In vitro, rhizolutin substantially decreased Aβ-induced apoptosis and inflammation in neuronal and glial cells. Our findings introduce a unique chemical entity that targets Aβ and tau concurrently by mimicking misfolded protein clearance mechanisms of immunotherapy, which is prominently investigated in clinical trials.

Keywords: Alzheimer's disease; amyloid β; lactones; natural products; tau protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alzheimer Disease / drug therapy*
  • Alzheimer Disease / pathology
  • Amyloid beta-Peptides / antagonists & inhibitors*
  • Amyloid beta-Peptides / metabolism
  • Animals
  • Apoptosis / drug effects*
  • Inflammation / drug therapy*
  • Inflammation / pathology
  • Mice
  • Mice, Transgenic
  • Neuroglia / drug effects
  • Neurons / drug effects
  • Neuroprotective Agents / chemistry
  • Neuroprotective Agents / isolation & purification
  • Neuroprotective Agents / pharmacology*
  • Plaque, Amyloid / drug therapy
  • Plaque, Amyloid / pathology
  • Protein Aggregates / drug effects
  • Streptomyces / chemistry
  • tau Proteins / antagonists & inhibitors*
  • tau Proteins / metabolism

Substances

  • Amyloid beta-Peptides
  • Neuroprotective Agents
  • Protein Aggregates
  • tau Proteins