2014年11月
Phosphorylation regulates fibrillation of an aggregation core peptide in the second repeat of microtubule-binding domain of human tau
BIOORGANIC & MEDICINAL CHEMISTRY
- ,
- ,
- ,
- ,
- ,
- ,
- 巻
- 22
- 号
- 22
- 開始ページ
- 6471
- 終了ページ
- 6480
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bmc.2014.09.032
- 出版者・発行元
- PERGAMON-ELSEVIER SCIENCE LTD
Hyperphosphorylation of the microtubule-associated protein tau is believed to play a crucial role in the neurofibrillary tangles formation in Alzheimer's disease brain. In this study, fibril formation of peptides containing the critical sequences for tau aggregation VQIINK and a plausible serine phosphorylation site of tau at its C-terminal was investigated. All the peptides formed fibrils with the typical cross-beta structural core. However, stability of the fibrils was highly sensitive to the pH conditions for the phosphorylated VQIINK peptide, suggesting a regulatory role of phosphorylation for the amyloid-formation of tau. (C) 2014 Elsevier Ltd. All rights reserved.
- リンク情報
- ID情報
-
- DOI : 10.1016/j.bmc.2014.09.032
- ISSN : 0968-0896
- eISSN : 1464-3391
- PubMed ID : 25440728
- Web of Science ID : WOS:000344472600018