Dissolution of β2-microglobulin amyloid fibrils by dimethylsulfoxide
Dissolution of β2-microglobulin amyloid fibrils by dimethylsulfoxide
复制标题
DOI：
10.1093/jb/mvg124
复制
发表时间：
2003-07-01
影响因子：
2.7
通讯作者：
Goto, Y
中科院分区：
文献类型：
--
作者：
Hirota-Nakaoka, N;Hasegawa, K;Goto, Y
越来越多的蛋白质被发现聚集成不溶性纤维，统称为淀粉样纤维。为了研究淀粉样蛋白纤维的构象稳定性，我们用圆二色谱、硫代黄素T荧光、光散射和电子显微镜研究了二甲基亚砜(DMSO)、2，2，2-三氟乙醇(TFE)和1，1，1，3，3，3-六氟-2-丙醇(HFIP)对β(2)-微球蛋白淀粉样纤维的影响。当用圆二向色性测量时。而硫代黄素T荧光、HFIP和TFE溶解了纤维，产生了主要的螺旋构象。然而，通过光散射和电子显微镜观察，这些醇并不能完全溶解淀粉样纤维。另一方面，DMSO完全溶解了淀粉样纤维，尽管需要高浓度[即80%(v/v)]。这些结果与氢键在稳定淀粉样纤维中的重要作用是一致的。
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 beta(2)-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.