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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概要
- 論文の詳細を見る
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 °C, hen egg white lysozyme, bovine β-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.
- 社団法人 日本農芸化学会の論文
- 2007-05-23
著者
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Shiraki Kentaro
Institute For Applied Physics University Of Tsukuba
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Takagi Masahiro
School Of Materials Science Japan Advanced Institute Of Science And Technology (jaist)
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Takagi Masahiro
School Of Material Science Japan Advanced Institute Of Science And Technology
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Aso Yoshikazu
School Of Material Science Japan Advanced Institute Of Science And Technology
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Aso Yoshikazu
School Of Materials Science Japan Advanced Institute Of Science And Technology (jaist)
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Shiraki Kentaro
Div. Of Applied Physics Graduate School Of Pure And Applied Sciences Univ. Of Tsukuba
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