Circular dichroism and aggregation studies of amyloid beta [11-28] fragment and its variants

• Autorzy: Juszczyk P. , Kolodziejczyk A.S. , Grzonka Z.
• Języki publikacji: EN

Abstrakty

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.

Słowa kluczowe

EN

Alzheimer's disease; amyloid beta; aggregation; dementia; circular dichroism; secondary structure; thioflavine T assay

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2005
• Tom: 52
• Numer: 2
• Opis fizyczny: p.425-431,fig.,ref.

Twórcy

autor

Juszczyk P.

• University of Gdansk, Gdansk, Poland

autor

Kolodziejczyk A.S.

autor

Grzonka Z.

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