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- Title
Dissolution of β<sup>2</sup>-Microglobulin Amyloid Fibrils by Dimethylsulfoxide.
- Authors
Hirota-Nakaoka, Nami; Hasegawa, Kazuhiro; Naiki, Hironobu; Goto, Yuji
- Abstract
Increasing numbers of proteins have been found to aggregate into insoluble fibers, collectively referred to as amyloid fibrils. To address the conformational stability of amyloid fibrils, we studied the effects of dimethylsulfoxide (DMSO), 2,2,2-trifluoroethanol (TFE), and 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) on β2-microglobulin amyloid fibrils by circular dichroism, thioflavin T fluorescence, light scattering, and electron microscopy. When measured by circular dichroism and thioflavin T fluorescence, HFIP, and TFE dissolved the fibrils, producing predominantly helical conformations. However, these alcohols did not dissolve the amyloid fibrils completely as monitored by light scattering and electron microscopy. On the other hand, DMSO completely dissolved the amyloid fibrils although a high concentration [i.e., 80% (v/v)] was required. These results are consistent with the important role of hydrogen bonds in stabilizing amyloid fibrils.
- Subjects
AMYLOID; DICHROISM; DIMETHYL sulfoxide; PROTEINS; BIOCHEMISTRY
- Publication
Journal of Biochemistry, 2003, Vol 134, Issue 1, p159
- ISSN
0021-924X
- Publication type
Article
- DOI
10.1093/jb/mvg124