Inhibiting and catalysing amyloid fibrillation at dynamic lipid interfaces

Proteins are naturally exposed to diverse interfaces in living organisms, from static solid to dynamic fluid. Solid interfaces can enrich proteins as corona, and then catalyze, retard or hinder amyloid fibrillation. But fluid interfaces abundant in biology have rarely been studied for their correlation with protein fibrillation. Unsaturated fatty acids own growing essential roles in diet, whose fluid interfaces are found in vitro to catalyze amyloid fibrillation under certain physiologic conditions. It is determined by the location of double bonds within alkyl chains as well as the presence of physical shear. Docosahexaenoic acid (DHA) shows low catalysis because its unique alkyl chain does not favor to stabilize cross-β nucleus. Mixtures of different fatty acids also decelerate their catalytic activity. High catalysis poses an unprecedented approach to synthesize biologic nanofibrils as one-dimensional (1D) building blocks of functional hybrids. Fibrillation inhibition implied that appropriate diet would be a preventive strategy for amyloid-related diseases. Thus these results may find their significances in diverse fields of science as chemistry, biotechnology, nanotechnology, nutrition, amyloid pathobiology and nanomedicine.