Amylum forms typical self-assembled amyloid fibrils

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.