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Amyloid protein fibrils are best known as bad actors in Alzheimer's and related diseases. But they can also serve functional roles, as bacterial coatings, for example, suggesting that amyloids might become useful as designed synthetic materials. Although the flexibility or rigidity of the fibrils varies over a range of four orders of magnitude, the factors determining such properties are not well-known. A major factor controlling this flexibility or rigidity turns out to be the fibrils' hydrogen-bonding networks, according to Christopher M. Dobson, Mark E. Welland, and coworkers at the University of Cambridge (Science 2007, 318, 1900). The researchers found that a key determinant of amyloid structure is the strength of H-bonds that form among stacked β-sheets in the common core structure of the highly ordered fibrils (shown, H-bonds are yellow). Variable side-chain interactions also have an important influence, but to a lesser degree. These conclusions could lead not only to a better understanding of the role of amyloid fibrils in disease but also to the greater use of such structures "both in biotechnology and as nanoscale materials," the researchers note.
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