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Comparative properties of Aβ1-42, Aβ11-42, and [Pyr¹¹]Aβ11-42 generated from O-acyl isopeptides.

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.
AuthorsYouhei Sohma, Moe Yamasaki, Hiroyuki Kawashima, Atsuhiko Taniguchi, Masayuki Yamashita, Kenichi Akaji, Hidehito Mukai, Yoshiaki Kiso
JournalBioorganic & medicinal chemistry letters (Bioorg Med Chem Lett) Vol. 23 Issue 5 Pg. 1326-9 (Mar 01 2013) ISSN: 1464-3405 [Electronic] England
PMID23352512 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
CopyrightCopyright © 2012 Elsevier Ltd. All rights reserved.
Chemical References
  • Amyloid beta-Peptides
  • Peptide Fragments
Topics
  • Alzheimer Disease (metabolism)
  • Amyloid beta-Peptides (chemistry)
  • Circular Dichroism
  • Humans
  • Peptide Fragments (chemical synthesis, chemistry)
  • Protein Structure, Secondary

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