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Peer-reviewedCC BY 4.0International Journal of Molecular Sciences

Sargassum horneri Fucoidan Suppresses the Early-Stage Amyloid Fibrillation of Insulin

  • Noriko Amishiro1
  • Asuka Miwa2
  • Shiho Kariya1
  • Yuka Ito2
  • Yukihiro Yasaski2
  • Minoru Funakoshi3
  • Takashi Ohshiro4,5,6
  • Hisashi Yagi4,5,6
6 affiliations
  1. 1Department of Engineering, Graduate School of Sustainability Science, Tottori University, 4-101 Koyamacho-minami, Tottori-city 680-8552, Tottori Prefecture, Japan
  2. 2Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, 4-101 Koyamacho-minami, Tottori-city 680-8552, Tottori Prefecture, Japan
  3. 3Marine Products KIMURAYA Co., Ltd., 3307 Wataricho, Sakaiminato-city 684-0072, Tottori Prefecture, Japan
  4. 4Department of Chemistry and Biotechnology, Faculty of Engineering, Tottori University, 4-101 Koyamacho-minami, Tottori-city 680-8552, Tottori Prefecture, Japan
  5. 5Center for Research on Green Sustainable Chemistry, Tottori University, 4-101 Koyamacho-minami, Tottori-city 680-8552, Tottori Prefecture, Japan
  6. 6Research Center for Utilization of Unused Biological Resources, Tottori University, 4-101 Koyamacho-minami, Tottori-city 680-8550, Tottori Prefecture, Japan
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Abstract

Amyloid fibril formation is implicated in numerous protein misfolding disorders. Fucoidan, a sulfated polysaccharide primarily derived from brown algae, exhibits diverse biological activities. In this study, we investigated the inhibitory effect of Sargassum horneri fucoidan (S-fucoidan) on insulin amyloid fibrillation in vitro. Initial screening of fucoidans derived from Cladosiphon okamuranus, Kjellmaniella crassifolia, and S. horneri identified S-fucoidan as the most effective inhibitor of insulin fibrillation. Therefore, we characterized the inhibitory effect of S-fucoidan using Thioflavin T fluorescence, transmission electron microscopy, circular dichroism spectroscopy, size-exclusion chromatography, and cell viability assays. Both S-fucoidan and low-molecular-weight S-fucoidan inhibited fibrillation in a concentration-dependent manner. When present from the onset of the reaction, S-fucoidan prevented detectable fibril formation, preserved the initial secondary structure of insulin, and maintained insulin in a monomeric or near-monomeric state. In contrast, addition during nucleation or elongation did not effectively halt ongoing fibrillation. These findings indicate that S-fucoidan predominantly suppresses the early stage of insulin amyloid fibrillation and provide a basis for investigating the molecular mechanisms underlying its anti-fibrillation activity.

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Cite

BibTeXRIS
BibTeX
@article{amishiro2026sargassum,
  title = {{Sargassum horneri Fucoidan Suppresses the Early-Stage Amyloid Fibrillation of Insulin}},
  author = {Noriko Amishiro and Asuka Miwa and Shiho Kariya and Yuka Ito and Yukihiro Yasaski and Minoru Funakoshi and Takashi Ohshiro and Hisashi Yagi},
  journal = {International Journal of Molecular Sciences},
  year = {2026},
  month = oct,
  doi = {10.3390/ijms27219516},
  url = {https://www.mdpi.com/1422-0067/27/21/9516},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Sargassum horneri Fucoidan Suppresses the Early-Stage Amyloid Fibrillation of Insulin
AU  - Noriko Amishiro
AU  - Asuka Miwa
AU  - Shiho Kariya
AU  - Yuka Ito
AU  - Yukihiro Yasaski
AU  - Minoru Funakoshi
AU  - Takashi Ohshiro
AU  - Hisashi Yagi
PY  - 2026
DA  - 2026/10/24
JO  - International Journal of Molecular Sciences
DO  - 10.3390/ijms27219516
UR  - https://www.mdpi.com/1422-0067/27/21/9516
AB  - Amyloid fibril formation is implicated in numerous protein misfolding disorders. Fucoidan, a sulfated polysaccharide primarily derived from brown algae, exhibits diverse biological activities. In this study, we investigated the inhibitory effect of Sargassum horneri fucoidan (S-fucoidan) on insulin amyloid fibrillation in vitro. Initial screening of fucoidans derived from Cladosiphon okamuranus, Kjellmaniella crassifolia, and S. horneri identified S-fucoidan as the most effective inhibitor of insulin fibrillation. Therefore, we characterized the inhibitory effect of S-fucoidan using Thioflavin T fluorescence, transmission electron microscopy, circular dichroism spectroscopy, size-exclusion chromatography, and cell viability assays. Both S-fucoidan and low-molecular-weight S-fucoidan inhibited fibrillation in a concentration-dependent manner. When present from the onset of the reaction, S-fucoidan prevented detectable fibril formation, preserved the initial secondary structure of insulin, and maintained insulin in a monomeric or near-monomeric state. In contrast, addition during nucleation or elongation did not effectively halt ongoing fibrillation. These findings indicate that S-fucoidan predominantly suppresses the early stage of insulin amyloid fibrillation and provide a basis for investigating the molecular mechanisms underlying its anti-fibrillation activity.
SN  - 1422-0067
ER  -