Dissolution of β2-Microglobulin Amyloid Fibrils by Dimethylsulfoxide
スポンサーリンク
概要
- 論文の詳細を見る
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.
- 社団法人 日本生化学会の論文
著者
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Naiki Hironobu
Department Of Pathology Fukui Medical University And Crest
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Hasegawa Kazuhiro
Department Of Internal Medicine School Of Medicine Keio University
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Goto Yuji
Institute For Protein Research Osaka Univ
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Hirota-Nakaoka Nami
Institute for Protein Research, Osaka University and CREST, Japan Science and Technology Corporation
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Hasegawa Kazuhiro
Department of Pathology, Fukui Medical University and CREST, Japan Science and Technology Corporation
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