FTIR spectroscopic studies on aggregation process of the β‐amyloid 11–28 fragment and its variants
作者:
Paulina Juszczyk,
Aleksandra S. Kołodziejczyk,
Zbigniew Grzonka,
期刊:
Journal of Peptide Science
(WILEY Available online 2009)
卷期:
Volume 15,
issue 1
页码: 23-29
ISSN:1075-2617
年代: 2009
DOI:10.1002/psc.1085
出版商: John Wiley&Sons, Ltd.
关键词: Alzheimer's disease;amyloid β;Aβ variants;FTIR spectroscopy;secondary structure studies;aggregation studies
数据来源: WILEY
摘要:
AbstractAggregation of Aβ peptides is a seminal event in Alzheimer's disease. Detailed understanding of the Aβ assembly process would facilitate the targeting and design of fibrillogenesis inhibitors. Here, conformational studies using FTIR spectroscopy 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 behavior of the peptide during aggregation provoked by the addition of water to Aβ(11–28) solution in hexafluoroisopropanol was compared with the properties of its variants corresponding to natural, clinically relevant mutants at positions 21–23 (A21G, E22K, E22G, E22Q and D23N). The results showed that the aggregation of the peptides proceedsviaa helical intermediate, and it is possible that the formation of α‐helical structures is preceded by creation of 310‐helix/310‐turn structures. Copyright © 2008 European Peptide Society and Jo
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