RTHLVFFARK-NH2: A potent and selective modulator on Cu2+-mediated amyloid-β protein aggregation and cytotoxicity

2018 ◽  
Vol 181 ◽  
pp. 56-64 ◽  
Author(s):  
Jie Meng ◽  
Huan Zhang ◽  
Xiaoyan Dong ◽  
Fufeng Liu ◽  
Yan Sun
Keyword(s):  
Protein Aggregation ◽  
Amyloid Β ◽  
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 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

scholarly journals Early amyloid β-protein aggregation precedes conformational change

2014 ◽  
Vol 50 (40) ◽  
pp. 5373-5375 ◽  
Author(s):  
Bogdan Barz ◽  
Olujide O. Olubiyi ◽  
Birgit Strodel
Keyword(s):  
Molecular Dynamics ◽  
Protein Aggregation ◽  
Molecular Dynamics Simulations ◽  
Conformational Change ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Dynamics Simulations

The aggregation of amyloid-β protein (1–42) is studied at experimental concentrations using all-atom molecular dynamics simulations.

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