Amyloid-Like Fibril Formation by Tachykinin Neuropeptides and Its Relevance to Amyloid β-Protein Aggregation and Toxicity

2012 ◽  
Vol 64 (1) ◽  
pp. 29-44 ◽  
Author(s):  
Pradeep K. Singh ◽  
Samir K. Maji
Keyword(s):  
Protein Aggregation ◽  
Amyloid Β ◽  
Fibril Formation ◽  
Amyloid Β Protein ◽  
Β Protein

Conjugation of RTHLVFFARK to human lysozyme creates a potent multifunctional modulator for Cu2+-mediated amyloid β-protein aggregation and cytotoxicity

2020 ◽  
Vol 8 (11) ◽  
pp. 2256-2268 ◽  
Author(s):  
Xi Li ◽  
Wenjuan Wang ◽  
Xiaoyan Dong ◽  
Yan Sun
Keyword(s):  
Protein Aggregation ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Human Lysozyme ◽  
Β Protein

Conjugation of alkaline decapeptide (RTHLVFFARK) to lysozyme creates a potent multifunctional modulator (R-hLys) for Cu2+-mediated amyloid β-protein aggregation and cytotoxicity.

scholarly journals The Tottori (D7N) and English (H6R) Familial Alzheimer Disease Mutations Accelerate Aβ Fibril Formation without Increasing Protofibril Formation

2006 ◽  
Vol 282 (7) ◽  
pp. 4916-4923 ◽  
Author(s):  
Yukiko Hori ◽  
Tadafumi Hashimoto ◽  
Yosuke Wakutani ◽  
Katsuya Urakami ◽  
Kenji Nakashima ◽  
...  
Keyword(s):  
Alzheimer Disease ◽  
Amyloid Fibril ◽  
Amyloid Β ◽  
Fibril Formation ◽  
Amyloid Β Protein ◽  
Protein Precursor ◽  
Amyloid Fibril Formation ◽  
Β Protein ◽  
Familial Alzheimer Disease ◽  
Aβ Production

A subset of Alzheimer disease cases is caused by autosomal dominant mutations in genes encoding the amyloid β-protein precursor or presenilins. Whereas some amyloid β-protein precursor mutations alter its metabolism through effects on Aβ production, the pathogenic effects of those that alter amino acid residues within the Aβ sequence are not fully understood. Here we examined the biophysical effects of two recently described intra-Aβ mutations linked to early-onset familial Alzheimer disease, the D7N Tottori-Japanese and H6R English mutations. Although these mutations do not affect Aβ production, synthetic Aβ(1-42) peptides carrying D7N or H6R substitutions show enhanced fibril formation. In vitro analysis using Aβ(1-40)-based mutant peptides reveal that D7N or H6R mutations do not accelerate the nucleation phase but selectively promote the elongation phase of amyloid fibril formation. Notably, the levels of protofibrils generated from D7N or H6R Aβ were markedly inhibited despite enhanced fibril formation. These N-terminal Aβ mutations may accelerate amyloid fibril formation by a unique mechanism causing structural changes of Aβ peptides, specifically promoting the elongation process of amyloid fibrils without increasing metastable intermediates.

Type IV collagen prevents amyloid β-protein fibril formation

Life Sciences ◽  
2002 ◽  
Vol 70 (13) ◽  
pp. 1555-1564 ◽  
Author(s):  
Yoichi Kiuchi ◽  
Yoshihiko Isobe ◽  
Kiyomi Fukushima
Keyword(s):  
Type Iv Collagen ◽  
Amyloid Β ◽  
Fibril Formation ◽  
Amyloid Β Protein ◽  
Type Iv ◽  
Β Protein ◽  
Protein Fibril

scholarly journals Role of Aromatic Side Chains in Amyloid β-Protein Aggregation

2012 ◽  
Vol 3 (12) ◽  
pp. 1008-1016 ◽  
Author(s):  
Risto Cukalevski ◽  
Barry Boland ◽  
Birgitta Frohm ◽  
Eva Thulin ◽  
Dominic Walsh ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Amyloid Β ◽  
Side Chains ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Aromatic Side Chains

scholarly journals Exogenous amyloidogenic proteins function as seeds in amyloid β-protein aggregation

2014 ◽  
Vol 1842 (4) ◽  
pp. 646-653 ◽  
Author(s):  
Kenjiro Ono ◽  
Ryoichi Takahashi ◽  
Tokuhei Ikeda ◽  
Mineyuki Mizuguchi ◽  
Tsuyoshi Hamaguchi ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Amyloidogenic Proteins ◽  
Β Protein
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