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2005 | 52 | 2 | 425-431
Article title

Circular dichroism and aggregation studies of amyloid β (11-8) fragment and its variants.

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EN
Abstracts
EN
Aggregation of Aβ peptides is a seminal event in Alzheimer's disease. Detailed understanding of Aβ assembly would facilitate the targeting and design of fibrillogenesis inhibitors. Here comparative conformational and aggregation studies using CD spectroscopy and thioflavine T fluorescence assay are presented. As a model peptide, the 11-28 fragment of Aβ was used. This model peptide is known to contain the core region responsible for Aβ aggregation. The structural and aggregational behaviour of the peptide was compared with the properties of its variants corresponding to natural, clinically relevant mutants at positions 21-23 (A21G, E22K, E22G, E22Q and D23N). In HFIP (hexafluoro-2-propanol), a strong α-helix inducer, the CD spectra revealed an unexpectedly high amount of β-sheet conformation. The aggregation process of Aβ(11-28) variants provoked by water addition to HFIP was found to be consistent with a model of an α-helix-containing intermediate. The aggregation propensity of all Aβ(11-28) variants was also compared and discussed.
Publisher

Year
Volume
52
Issue
2
Pages
425-431
Physical description
Dates
published
2005
received
2005-04-12
revised
2005-06-03
accepted
2005-06-15
(unknown)
2005-06-25
Contributors
  • Department of Organic Chemistry, Faculty of Chemistry, University of Gdańsk, Gdańsk, Poland
  • Department of Organic Chemistry, Faculty of Chemistry, University of Gdańsk, Gdańsk, Poland
  • Department of Organic Chemistry, Faculty of Chemistry, University of Gdańsk, Gdańsk, Poland
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv52i2p425kz
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