Abstract
The secondary structure of a synthetic amyloid fragment des [Ala21,30]A42 was studied by circular dichroism and Fourier transformed infrared spectroscopy. Measurements were performed in trifluoroethanol/water and octyl β-d-glucopyranoside solutions. The spectra of the peptide in trifluoroethanol indicate a high percentage of a-helical structure. However, in octyl glucoside, at and above the critical micelle concentration, the peptide adopts a β-sheet conformation. Secondary structure analysis yields a predominant (> 70 %) β-sheet content. Our data suggest that the peptide backbone or polar side groups of des[Ala21,30]A42 interact with the sugar-coated surface of micelles, which promotes an a to β conformational transition.
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Laczkó-Hollósi, I., Hollósi, M., Lee, V.MY. et al. Conformational change of a synthetic amyloid analogue des[Ala21,3O]A42 upon binding to octyl glucoside micelles. Eur Biophys J 21, 345–348 (1992). https://doi.org/10.1007/BF00188347
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DOI: https://doi.org/10.1007/BF00188347