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• W2017884518 endingPage "14" @default.
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• W2017884518 abstract "The misfolding of the amyloid peptide, which is the result of a well-known α-to-β transition, causes neurodegenerative disorder. Fluorinated alcohols have been described in the literature as potent solvents which can refold the β-conformation. The present studies demonstrate the effectiveness of differently fluorinated alcohols for the β-to-α refolding process on fibrillar aggregated amyloid β(1–40). The regenerated helical structure is shown to be maintained in the absence of the fluoroalcohols, a behaviour which was found to contrast with immunoglobulin. We interpret this difference on the basis of the hydrophilic/hydrophobic domains in the amyloid sequence and present some speculations regarding the free-energy levels of the folded states of both proteins. The effect of the –CF3 group on the observed conformational changes is interpreted as a result of alterations of the hydration shell of the peptides. Moreover, based on the results achieved with fluoroalcohols, we have used novel fluorinated amphiphiles possessing blood-compatibility properties and studied their effect on amyloid β(1–40). First results point in the direction of a β-to-α transition. Therefore, the use of fluorine groups in the development of new drugs is considered a new possibility requiring further investigation for the prevention of amyloidosis." @default.
• W2017884518 created "2016-06-24" @default.
• W2017884518 creator A5019619893 @default.
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• W2017884518 date "2003-01-01" @default.
• W2017884518 modified "2023-10-16" @default.
• W2017884518 title "Change and stabilization of the amyloid-β(1–40) secondary structure by fluorocompounds" @default.
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• W2017884518 doi "https://doi.org/10.1016/s1570-9639(02)00461-2" @default.
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