Solution NMR structure and inhibitory effect against amyloid-β fibrillation of Humanin containing a d-isomerized serine residue

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Solution NMR structure and inhibitory effect against amyloid-β fibrillation of Humanin containing a d-isomerized serine residue

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作者：Nesreen Alsanousi^a ; ¹ ; Toshihiko Sugiki^a ; ¹ ; ^{sugiki@protein.osaka-u.ac.jp" class="auth_mail" title="E-mail the corresponding author} ; Kyoko Furuita^a ; Masatomo So^a ; Young-Ho Lee^a ; Toshimichi Fujiwara^a ; Chojiro Kojima^a ; ^b ; ^{kojima-chojiro-xk@ynu.ac.jp" class="auth_mail" title="E-mail the corresponding author}
关键词：Humanin ; d-isomerization ; NMR spectroscopy ; Alzheimer's disease ; Amyloid-β
刊名：Biochemical and Biophysical Research Communications
出版年：2016
出版时间：2 September 2016
年：2016
卷：477
期：4
页码：647-653
全文大小：2040 K

文摘

•: Humanin d-Ser14 showed the strongest inhibitory activity against Aβ40 fibrillation.
•: NMR structure of Humanin d-Ser14 was determined in alcohol/water mixture solution.
•: Humanin d-Ser14 directly bound Aβ40 stronger than Humanin wild-type and Humanin S14G.
•: Aβ40 and zinc ion binding sites of Humanin d-Ser14 were identified.
•: Structure around Ser14 of Humanin is critical for Aβ40 binding and inhibitory activity.

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