Conformational change of a synthetic amyloid analogue des[Ala21,3O]A42 upon binding to octyl glucoside micelles
✍ Scribed by Ilona Laczkó-Hollósi; Miklós Hollósi; Virginia M.-Y. Lee; Henry H. Mantsch
- Book ID
- 104656209
- Publisher
- Springer
- Year
- 1992
- Tongue
- English
- Weight
- 444 KB
- Volume
- 21
- Category
- Article
- ISSN
- 1432-1017
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✦ Synopsis
The secondary structure of a synthetic amyloid fragment des [AlaZL3°]A42 was studied by circular dichroism and Fourier transformed infrared spectroscopy. Measurements were performed in trifluoroethanol/water and octyl /?-D-glucopyranoside solutions. The spectra of the peptide in trifluoroethanol indicate a high percentage of c~-helical structure. However, in octyl glucoside, at and above the critical micelle concentration, the peptide adopts a/~-sheet conformation. Secondary structure analysis yields a predominant (> 70 %)/3-sheet content. Our data suggest that the peptide backbone or polar side groups of des[Ala21'3°]A42 interact with the sugar-coated surface of micelles, which promotes an c~ to/3 conformational transition.