Systematic analysis of aggregates from 38 kinds of non disease-related proteins: Identifying the intrinsic propensity of polypeptides to form amyloid fibrils
Systematic analysis of aggregates from 38 kinds of non disease-related proteins: Identifying the intrinsic propensity of polypeptides to form amyloid fibrils
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DOI：
10.1271/bbb.60718
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发表时间：
2007-05-01
影响因子：
1.6
通讯作者：
Takagi, Masahiro
中科院分区：
文献类型：
--
作者：
Aso, Yoshikazu;Shiraki, Kentaro;Takagi, Masahiro
从广泛的蛋白质中形成淀粉样纤维的能力将为增加淀粉样纤维形成的分子基础的研究提供机会。我们研究了36种不同的条件下，相对于四个模型蛋白质，以评估他们的能力，形成淀粉样纤维。在57 ℃、pH2的5%乙醇溶液中，鸡蛋白色溶菌酶、牛FL-乳球蛋白和牛胰蛋白酶原形成成熟型原纤维，而只有组蛋白H2A形成未成熟型原纤维。在这些条件下，38种蛋白质中的25种形成淀粉样纤维。此外，另外三种蛋白质在含有5%三氟乙醇而不是5%乙醇的溶液中形成原纤维。总之，总共有28种蛋白质形成淀粉样纤维。在这些极端条件下，观察到化学碎裂。天然结构的不稳定、氢键的加强和化学断裂被认为在淀粉样纤维的形成中起重要作用。
The ability to form amyloid fibrils from a wide range of proteins would open up the opportunity to augment studies of the molecular basis of amyloid fibril formation. We investigated 36 different conditions with respect to four model proteins to evaluate their ability to form amyloid fibrils. In a 5% ethanol solution at pH 2 at 57 degrees C, hen egg white lysozyme, bovine fl-lactoglobulin, and bovine trypsinogen formed mature-type fibrils, while only histone H2A formed immature-type fibrils. Under these conditions, 25 of the 38 proteins formed amyloid fibrils. In addition, three additional proteins formed fibrils in a solution containing 5% trifluoroethanol instead of 5% ethanol. In summary, a total 28 proteins formed amyloid fibrils. Under these extreme conditions, chemical fragmentation was observed. Destabilization of the native structure, strengthening of hydrogen bonds, and chemical fragmentation are thought to play important roles in the formation of amyloid fibrils.