scholarly journals Charge states rather than propensity for β-structure determine enhanced fibrillogenesis in wild-type Alzheimer's β-amyloid peptide compared to E22Q Dutch mutant

2009 ◽  
Vol 11 (7) ◽  
pp. 1639-1647 ◽  
Author(s):  
Francesca Massi ◽  
D. Klimov ◽  
D. Thirumalai ◽  
John E. Straub
Keyword(s):  
Amyloid Peptide ◽  
Wild Type ◽  
Β Amyloid ◽  
Charge States ◽  
Β Amyloid Peptide

scholarly journals Conformational Characterization of Native and L17A/F19A-Substituted Dutch-Type β-Amyloid Peptides

2020 ◽  
Vol 21 (7) ◽  
pp. 2571 ◽  
Author(s):  
Kai-Cyuan He ◽  
Yi-Ru Chen ◽  
Chu-Ting Liang ◽  
Shi-Jie Huang ◽  
Chung-Ying Tzeng ◽  
...  
Keyword(s):  
Sodium Dodecyl ◽  
Amyloid Peptide ◽  
Genetic Mutations ◽  
Wild Type ◽  
Amyloid Peptides ◽  
Aβ Aggregation ◽  
Nuclear Magnetic Spectroscopy ◽  
Β Amyloid ◽  
Β Amyloid Peptide

Some mutations which occur in the α/β-discordant region (resides 15 to 23) of β-amyloid peptide (Aβ) lead to familial Alzheimer’s disease (FAD). In vitro studies have shown that these genetic mutations could accelerate Aβ aggregation. We recently showed that mutations in this region could alter the structural propensity, resulting in a different aggregative propensity of Aβ. Whether these genetic mutations display similar effects remains largely unknown. Here, we characterized the structural propensity and aggregation kinetics of Dutch-type Aβ40 (Aβ40(E22Q)) and its L17A/F19A-substituted mutant (Aβ40(L17A/F19A/E22Q)) using circular dichroism spectroscopy, nuclear magnetic spectroscopy, and thioflavin T fluorescence assay. In comparison with wild-type Aβ40, we found that Dutch-type mutation, unlike Artic-type mutation (E22G), does not reduce the α-helical propensity of the α/β-discordant region in sodium dodecyl sulfate micellar solution. Moreover, we found that Aβ40(L17A/F19A/E22Q) displays a higher α-helical propensity of the α/β-discordant region and a slower aggregation rate than Aβ40(E22Q), suggesting that the inhibition of aggregation might be via increasing the α-helical propensity of the α/β-discordant region, similar to that observed in wild-type and Artic-type Aβ40. Taken together, Dutch-type and Artic-type mutations adopt different mechanisms to promote Aβ aggregation, however, the L17A/F19A mutation could increase the α-helical propensities of both Dutch-type and Artic-type Aβ40 and inhibit their aggregation.

N2L, a novel lipoic acid-niacin dimer protects HT22 cells against β-amyloid peptide-induced damage through attenuating apoptosis

2019 ◽  
Vol 34 (6) ◽  
pp. 1761-1770 ◽  
Author(s):  
Rikang Wang ◽  
Lang Zhang ◽  
Rifang Liao ◽  
Qian Li ◽  
Rongbiao Pi ◽  
...  
Keyword(s):  
Lipoic Acid ◽  
Amyloid Peptide ◽  
Ht22 Cells ◽  
Β Amyloid ◽  
Β Amyloid Peptide

scholarly journals Mutagenic analysis of the nucleation propensity of oxidized Alzheimer's β-amyloid peptide

2005 ◽  
Vol 14 (8) ◽  
pp. 2125-2131 ◽  
Author(s):  
Tony Christopeit ◽  
Peter Hortschansky ◽  
Volker Schroeckh ◽  
Karlheinz Gührs ◽  
Giorgia Zandomeneghi ◽  
...  
Keyword(s):  
Amyloid Peptide ◽  
Β Amyloid ◽  
Β Amyloid Peptide

Inhibitors of Fibril Formation and Cytotoxicity of β-Amyloid Peptide Composed of KLVFF Recognition Element and Flexible Hydrophilic Disrupting Element

2002 ◽  
Vol 290 (1) ◽  
pp. 121-124 ◽  
Author(s):  
Ken-ichi Watanabe ◽  
Kazuhiko Nakamura ◽  
Shingo Akikusa ◽  
Tomoko Okada ◽  
Masato Kodaka ◽  
...  
Keyword(s):  
Fibril Formation ◽  
Amyloid Peptide ◽  
Recognition Element ◽  
Β Amyloid ◽  
Β Amyloid Peptide
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