Template-Directed Self-Assembly and Growth of Insulin Amyloid Fibrils

The study developed a novel synthetic amyloid template to facilitate the study of amyloid deposition, a process critical in neurodegenerative diseases and type II diabetes. By covalently attaching amyloid seeds to an N-hydroxysuccinimide-activated surface, researchers used insulin as a model protein to observe fibril formation. The synthetic template allowed for rapid fibril growth without lag time, producing long, thin fibrils due to limited nucleation sites and lack of lateral twisting. Techniques such as thioflavin T-induced fluorescence and Congo red binding confirmed the fibrils as amyloids formed through conformational rearrangement of insulin monomers. The deposition rate followed saturation kinetics with insulin concentration, aligning with previous human studies. This synthetic template could be used for screening amyloid deposition inhibitors in vitro.