Journal
COLLOIDS AND SURFACES B-BIOINTERFACES
Volume 229, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.colsurfb.2023.113481
Keywords
Amyloid; Aggregation; Surfactant; Neurodegenerative; Bovine liver catalase
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The study investigated the effect of anionic surfactant SDS on the fibrillation of BLC under acidic conditions. Various methods were used to evaluate the conformational changes of BLC in response to SDS treatment. The results showed that low concentrations of SDS induced a transition from random coil to native-like structure, while high concentrations led to aggregation and formation of cross beta-sheeted structure in BLC.
The mechanism by which anionic surfactants promote amyloid fibril is not well understood. Here, we investigated how sodium dodecyl sulfate (SDS), a negatively charged surfactant, affects the fibrillation of the partially unfolded random-coiled bovine liver catalase (BLC) at a pH of 2.0. We used several methods, including turbidity, RLS kinetics, intrinsic fluorescence, ThT fluorescence, far-UV CD, and TEM imaging, to evaluate the conformational changes of BLC in vitro in response to SDS treatment. BLC is a multimeric protein and well folded at physiological pH but forms a random coil structure at pH 2.0. Intrinsic fluorescence and far-UV CD data showed that below 0.1 mM SDS, random coiled BLC turned into a native-like structure. BLC incubated with an SDS concentration ranging from 0.1 to 2.0 mM led to the formation of aggregates. The ThT fluorescence intensity was enhanced in the aggregated BLC samples (0.1-2.0 mM SDS), and cross beta-sheeted structure was detected by the far UV CD measurements. BLC adopts a complete alpha-helical structure upon interacting with SDS at a more than 2.0 mM concentration at pH 2.0. Understanding the mechanism of surfactant-or lipid-induced fibrillation is important for therapeutic purposes.
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