- Tytuł:
- Circular dichroism and aggregation studies of amyloid β (11-8) fragment and its variants.
- Autorzy:
-
Juszczyk, Paulina
Kołodziejczyk, Aleksandra
Grzonka, Zbigniew - Powiązania:
- https://bibliotekanauki.pl/articles/1041423.pdf
- Data publikacji:
- 2005
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
secondary structure studies
thioflavine T assay
aggregation studies.
Alzheimer's disease
amyloid β
circular dichroism (CD) - Opis:
- 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.
- Źródło:
-
Acta Biochimica Polonica; 2005, 52, 2; 425-431
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki
Artykuł