Amyloid-forming propensity of the hydrophobic non-natural amino acid on the fibril-forming core peptide of human tau
Amyloid-forming propensity of the hydrophobic non-natural amino acid on the fibril-forming core peptide of human tau
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DOI：
10.1016/j.bmcl.2007.03.071
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发表时间：
2007-06-01
影响因子：
2.7
通讯作者：
Morii, Takashi
中科院分区：
文献类型：
--
作者：
Hirata, Akiyoshi;Sugimoto, Kenji;Morii, Takashi
已知具有芳香族侧链的氨基酸残基，如Tyr和Phe，通过影响致病多肽的淀粉样蛋白形成倾向，在形成和稳定致病多肽的淀粉样蛋白原纤维中发挥重要作用。我们研究了含有非天然氨基酸的肽的淀粉样蛋白型聚集，所述非天然氨基酸来源于人类致病蛋白tau的核心部分。联苯基的疏水性质及其分子间芳香相互作用强烈改变其淀粉样蛋白形成性质。(C)2007爱思唯尔有限公司版权所有。
Amino acid residues with aromatic side chains, such as Tyr and Phe, are known to play essential roles in forming and stabilizing the amyloid fibrils of pathogenic polypeptides by affecting their amyloid forming propensity. We have studied the amyloid-type aggregation of peptides containing non-natural amino acid derived from a core part of human pathogenic protein, tau. The hydrophobic nature of the biphenyl group and its intermolecular aromatic interactions strongly alter their amyloid formation properties. (C) 2007 Elsevier Ltd. All rights reserved.