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- W2201426077 abstract "It is well known that amyloid fibrils are associated with a lot of neurodegenerative diseases. Thus, inhibition of protein aggregation and disruption of the formed amyloid fibrils have been attractive therapeutic strategies for amyloid-associated diseases. Here, we take the widely studied protein, β-lactoglobulin (β-LG), as a model protein to study the inhibition of amyloid fibrils. Using multiple biophysical and biochemical approaches, we successfully identify that folic acid can strongly inhibit amyloid fibrils formation of β-LG in 5 M urea solution. In the presence of folic acid, both the nucleation step and elongation step of β-LG fibrillation can be affected and the suppression efficiency followed a dose depended manner. Furthermore, the studies of protein intrinsic-fluorescence and anilinonaphthalene-8-sulfonic acid (ANS) fluorescence demonstrated that the folic acid decreased the hydrophobicity of the urea-denatured β-LG and changed the conformation of β-LG. Our study provides a convenient way to inhibit the amyloid fibrils formation, which has potential help to study the mechanism of amyloid-diseases." @default.
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- W2201426077 date "2017-02-10" @default.
- W2201426077 modified "2023-09-22" @default.
- W2201426077 title "Folic acid inhibits the amyloid fibrils formation of β-lactoglobulin" @default.
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- W2201426077 doi "https://doi.org/10.18088/ejbmr.1.1.2015.pp22-27" @default.
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