Abstract |
The use of water-soluble O-acyl isopeptides enabled us to investigate the biochemical properties of Aβ11-42 species, by preparing highly concentrated stock solutions after a pretreatment. Aβ11-42 and [Pyr(11)]Aβ11-42 showed comparable aggregation capability and cytotoxicity, suggesting that the pyroglutamate modification at Glu(11) does not have a crucial role in these events. However, given that Aβ11-42 is converted to [Pyr(11)]Aβ11-42 by a glutamyl cyclase in vivo, the potential aggregative and cytotoxic nature of [Pyr(11)]Aβ11-42 that was observed in the present study provides valuable insights into the pathological functions of pyroglutamate-modified Aβ species in Alzheimer's disease.
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Authors | Youhei Sohma, Moe Yamasaki, Hiroyuki Kawashima, Atsuhiko Taniguchi, Masayuki Yamashita, Kenichi Akaji, Hidehito Mukai, Yoshiaki Kiso |
Journal | Bioorganic & medicinal chemistry letters
(Bioorg Med Chem Lett)
Vol. 23
Issue 5
Pg. 1326-9
(Mar 01 2013)
ISSN: 1464-3405 [Electronic] England |
PMID | 23352512
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | Copyright © 2012 Elsevier Ltd. All rights reserved. |
Chemical References |
- Amyloid beta-Peptides
- Peptide Fragments
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Topics |
- Alzheimer Disease
(metabolism)
- Amyloid beta-Peptides
(chemistry)
- Circular Dichroism
- Humans
- Peptide Fragments
(chemical synthesis, chemistry)
- Protein Structure, Secondary
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