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 -CF 3 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.