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

The study explored the formation of insulin amyloid fibrils using a novel synthetic amyloid template, which mimicked natural amyloid deposition processes. By covalently attaching amyloid seeds to an N-hydroxysuccinimide-activated surface, researchers observed that insulin monomers formed fibrils on this template without a lag time and at an accelerated rate compared to in solution. These fibrils were over 2 μm long and thinner due to limited nucleation sites and lack of lateral twisting. The fibrils were confirmed as amyloids through various assays, and the deposition rate followed saturation kinetics with insulin concentration. This synthetic template was proposed as a tool for screening amyloid deposition inhibitors in vitro, aligning with characteristics observed in human amyloid plaque studies.