Sulfated polysaccharide ascophyllan prevents amyloid fibril formation of human insulin and inhibits amyloid-induced hemolysis and cytotoxicity in PC12 cells. Issue 11 (14th September 2021)

• Record Type: Journal Article
• Authors: Liang, Yan; Ueno, Mikinori; Zha, Shijiao; Okimura, Takasi; Jiang, Zedong; Yamaguchi, Kenichi; Hatakeyama, Tomomitsu; Oda, Tatsuya
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 85:Issue 11(2021)
• Page Start: 2281
• Page End: 2291
• Publication Date: 2021-09-14
• Subjects: Ascophyllum nodosum -- ascophyllan -- amyloid formation -- insulin; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1093/bbb/zbab163
• Languages: English
• ISSNs: 0916-8451

Abstract

ABSTRACT: We found that ascophyllan significantly inhibited the fibrillation of human insulin and was the most effective among the sulfated polysaccharides tested. Gel-filtration analysis suggested that ascophyllan was capable of forming a complex with insulin through a weak interaction. Secondary structure transition from native α-helix to β-sheet predominant structure of insulin under the fibrillation conditions was suppressed in the presence of ascophyllan. Interestingly, ascophyllan attenuated insulin fibril-induced hemolysis of human erythrocytes. Moreover, ascophyllan attenuated insulin amyloid-induced cytotoxicity on rat pheochromocytoma PC12 cells and reduced the level of intracellular reactive oxygen species. This is the first report indicating that a sulfated polysaccharide, ascophyllan, can suppress the insulin amyloid fibril formation and inhibit the fibril-induced detrimental bioactivities. Graphical Abstract: