Formation of α‐synuclein aggregates in aqueous ethylammonium nitrate solutions
Formation of α‐synuclein aggregates in aqueous ethylammonium nitrate solutions
复制标题
硝酸乙铵水溶液中 α-突触核蛋白聚集体的形成
DOI：
10.1002/bip.23352
复制
发表时间：
2020
期刊：
影响因子：
2.9
通讯作者：
Yoshimura Yukihiro
中科院分区：
文献类型：
--
作者：
Takekiyo Takahiro;Yamada Natsuki;Nakazawa Chikako T.;Amo Taku;Asano Atsushi;Yoshimura Yukihiro
研究了添加硝酸乙铵 (EAN)（一种离子液体 (IL)）对水溶液中 α-突触核蛋白 (α-Syn) 聚集体形成的影响。 FTIR 和拉曼光谱用于研究 α-Syn 二级结构以及水分子和 EAN 状态的变化。本文的结果表明，将 EAN 添加到 α-Syn 会导致分子间 β-折叠结构以以下方式形成：天然无序状态→→→聚脯氨酸 II (PPII)-螺旋→→分子间 β-折叠（α-Syn 淀粉样蛋白样聚集体：α-SynA）。尽管 EAN 的阳离子和阴离子在掩盖 α-SynA 形成过程中的带电侧链和 PPII 螺旋形成能力方面发挥着作用，但水分子与其形成没有直接关系。我们得出的结论是，在掩盖 α-Syn N 端和 C 端的带电侧链后，EAN 诱导的 α-Syn 淀粉样蛋白样聚集体在分子中间的疏水缔合处形成。
The effect of adding ethylammonium nitrate (EAN), which is an ionic liquid (IL), on the aggregate formation of α‐synuclein (α‐Syn) in aqueous solution has been investigated. FTIR and Raman spectroscopy were used to investigate changes in the secondary structure of α‐Syn and in the states of water molecules and EAN. The results presented here show that the addition of EAN to α‐Syn causes the formation of an intermolecular β‐sheet structure in the following manner: native disordered state → polyproline II (PPII)‐helix → intermolecular β‐sheet (α‐Syn amyloid‐like aggregates: α‐SynA). Although cations and anions of EAN play roles in masking the charged side chains and PPII‐helix‐forming ability involved in the formation of α‐SynA, water molecules are not directly related to its formation. We conclude that EAN‐induced α‐Syn amyloid‐like aggregates form at hydrophobic associations in the middle of the molecules after masking the charged side chains at the N‐ and C‐terminals of α‐Syn.