ArticleScience advances2024
Amylum forms typical self-assembled amyloid fibrils.
Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Assembly of resistant starch type 5 in two amylose matrices: effects of fatty acid chain length and matrix background on structural characteristics.Food chemistry: X · 2026Article
- Fabrication and antibacterial properties of self-assembled lysozyme nanofilms induced by reduced glutathione.Current research in food science · 2026Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibril formation is a central biochemical process in pathology and physiology. Over decades, substantial advances were made in elucidating the mechanisms of amyloidogenesis, its links to disease, and the production of functional supramolecular structures. While the term "amyloid" denotes starch-like features of these assemblies, no evidence of amyloidogenic behavior of polysaccharides has been so far reported. Here, we investigate the potential of amylum (starch) not only to self-assemble into hierarchical fibrillar structures but also to exhibit canonical amyloidogenic properties. Ordered amylum structures were formed through a sigmoidal growth process with characteristic amyloid features including typical nanofibril morphology, binding to indicative dyes, inherent luminescence, apple-green birefringence upon Congo red staining, and notable mechanical rigidity. These findings shed light on polysaccharide self-assembly and expand the generic amyloid phenomenon.
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