Anti-Parallel β-Hairpin Structure in Soluble Aβ Oligomers of Aβ40-Dutch and Aβ40-Iowa.
Anti-Parallel β-Hairpin Structure in Soluble Aβ Oligomers of Aβ40-Dutch and Aβ40-Iowa.
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DOI：
10.3390/ijms22031225
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发表时间：
2021-01-27
影响因子：
5.6
通讯作者：
Smith SO
中科院分区：
文献类型：
--
作者：
Fu Z;Van Nostrand WE;Smith SO
The amyloid-β (Aβ) peptides are associated with two prominent diseases in the brain, Alzheimer’s disease (AD) and cerebral amyloid angiopathy (CAA). Aβ42 is the dominant component of cored parenchymal plaques associated with AD, while Aβ40 is the predominant component of vascular amyloid associated with CAA. There are familial CAA mutations at positions Glu22 and Asp23 that lead to aggressive Aβ aggregation, drive vascular amyloid deposition and result in degradation of vascular membranes. In this study, we compared the transition of the monomeric Aβ40-WT peptide into soluble oligomers and fibrils with the corresponding transitions of the Aβ40-Dutch (E22Q), Aβ40-Iowa (D23N) and Aβ40-Dutch, Iowa (E22Q, D23N) mutants. FTIR measurements show that in a fashion similar to Aβ40-WT, the familial CAA mutants form transient intermediates with anti-parallel β-structure. This structure appears before the formation of cross-β-sheet fibrils as determined by thioflavin T fluorescence and circular dichroism spectroscopy and occurs when AFM images reveal the presence of soluble oligomers and protofibrils. Although the anti-parallel β-hairpin is a common intermediate on the pathway to Aβ fibrils for the four peptides studied, the rate of conversion to cross-β-sheet fibril structure differs for each.
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影响因子：
2.9
作者：
Fu, Ziao;Aucoin, Darryl;Smith, Steven
通讯作者：
Smith, Steven
影响因子：
4.8
作者：
Castano, EM;Prelli, F;Frangione, B
通讯作者：
Frangione, B
影响因子：
3.5
作者：
JOHNSTON, JA;COWBURN, RF;ONEILL, C
通讯作者：
ONEILL, C
DOI：
10.1073/pnas.0711731105
发表时间：
2008-04-01
影响因子：
11.1
作者：
Hoyer, Wolfgang;Gronwall, Caroline;Hard, Torleif
通讯作者：
Hard, Torleif
影响因子：
15
作者：
Paul, C;Wang, JP;Axelsen, PH
通讯作者：
Axelsen, PH