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J. Biochem, 2003, Vol. 134, No. 1 159-164
© 2003 Japanese Biochemical Society

BIOCHEMISTRY

Dissolution of ß2-Microglobulin Amyloid Fibrils by Dimethylsulfoxide

Nami Hirota-Nakaoka1, Kazuhiro Hasegawa2, Hironobu Naiki2 and Yuji Goto+,1

1 Institute for Protein Research, Osaka University and CREST, Japan Science and Technology Corporation, Suita, Osaka 565-0871; and 2 Department of Pathology, Fukui Medical University and CREST, Japan Science and Technology Corporation, Matsuoka, Fukui 910-1193

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 ß2-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.

+ To whom correspondence should be addressed. Tel: +81-6-6879-8614, Fax: +81-6-6879-8616, E-mail: ygoto{at}protein.osaka-u.ac.jp


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