Seven undescribed meroterpenoids from Sargassum siliquastrum and their inhibitory activity against amyloid β aggregation

J Nat Med. 2025 Jan;79(1):73-81. doi: 10.1007/s11418-024-01847-6. Epub 2024 Oct 15.

Abstract

The inhibition of amyloid β (Aβ) aggregation and degradation of Aβ aggregates are promising approaches for treating and preventing Alzheimer's disease. In our search for Aβ42 aggregation inhibitors, we isolated seven undescribed meroterpenoids, sargasilides A (1)‒G (7), from brown alga (Sargassum siliquastrum) collected at Noto Peninsula in Japan. We structurally elucidated the isolated meroterpenoids using spectroscopic data and evaluated their activities using Thioflavin T assay and transmission electron microscopy. Among the seven compounds isolated, sargasilide B had the strongest inhibitory activity. From the comparison of structure and activity, the geometric isomerism of olefins and length of isoprene side chains are important for the activity of meroterpenoids isolated from brown alga.

Keywords: Sargassum siliquastrum; Alzheimer’s disease; Amyloid β; Brown alga; Meroterpenoid.

MeSH terms

  • Alzheimer Disease / drug therapy
  • Amyloid beta-Peptides* / antagonists & inhibitors
  • Amyloid beta-Peptides* / metabolism
  • Humans
  • Japan
  • Molecular Structure
  • Peptide Fragments
  • Protein Aggregates / drug effects
  • Sargassum* / chemistry
  • Terpenes* / chemistry
  • Terpenes* / isolation & purification
  • Terpenes* / pharmacology

Substances

  • Amyloid beta-Peptides
  • Terpenes
  • Protein Aggregates
  • amyloid beta-protein (1-42)
  • Peptide Fragments