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Structural models have predicted that amyloid fibrils, which are associated with and may help cause conditions such as Alzheimer’s disease, grow symmetrically at both ends. Caryn L. Heldt, Shuqi Zhang, and Georges Belfort at Rensselaer Polytechnic Institute have put those models to the test and found them wanting (Proteins: Struct., Funct., Bioinf., DOI: 10.1002/prot.22861). The researchers attached different fluorescent dyes to the protein insulin, which forms amyloid, and to insulin-based fibrils. They then added the two together and used fluorescence to observe how the fibrils grew. “To our surprise, unidirectional growth for insulin fibrils was dominant,” Belfort says. About half of the fibrils behaved this way, about one-fifth grew bidirectionally, and more than a quarter didn’t grow. The findings could have implications for drug screening or drug design, as amyloid therapeutics often aim to inhibit fibril formation or break up existing fibrils. “There are no widely accepted molecular explanations for more than 20 amyloid diseases, and our work adds one small piece to the puzzle,” Belfort says.
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