Differential efficacy of lipophilic and cytosolic antioxidants on generation of reactive oxygen species by amyloid-β

2001 ◽  
Vol 3 (6) ◽  
pp. 525-529 ◽  
Author(s):  
Sirikarnt Dhitavat ◽  
E.R. Rivera ◽  
Eugene Rogers ◽  
Thomas B. Shea
Keyword(s):  
Reactive Oxygen Species ◽  
Amyloid Β ◽  
Reactive Oxygen ◽  
Oxygen Species

Inhibition and disaggregation of amyloid β protein fibrils through conjugated polymer–core thermoresponsive micelles

2020 ◽  
Vol 8 (44) ◽  
pp. 10126-10135
Author(s):  
Hao Geng ◽  
Hongbo Yuan ◽  
Liang Qiu ◽  
Dong Gao ◽  
Yongqiang Cheng ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
White Light ◽  
Conjugated Polymer ◽  
Amyloid Β ◽  
Reactive Oxygen ◽  
Light Irradiation ◽  
Amyloid Β Protein ◽  
Oxygen Species ◽  
Β Protein ◽  
Protein Fibrils

The micelles (CPMs) have a thermoresponsive surface and reactive oxygen species (ROS) generating core. At 37 °C, CPMs captured Aβ aggregates to inhibit and disaggregate aggregates under white-light irradiation, reducing Aβ-induced cytotoxicity.

Modelling Copper Binding to the Amyloid-β Peptide in Alzheimer

2010 ◽  
Vol 63 (3) ◽  
pp. 345 ◽  
Author(s):  
V. Chandana Epa ◽  
Victor A. Streltsov ◽  
Joseph N. Varghese
Keyword(s):  
Reactive Oxygen Species ◽  
Binding Site ◽  
Reactive Oxygen Species Generation ◽  
Computational Modelling ◽  
Amyloid Β ◽  
Reactive Oxygen ◽  
Oxidative Modification ◽  
Amyloid Β Peptide ◽  
Oxygen Species ◽  
Copper Binding

Oxidative modification due to reactive oxygen species generated by Cu2+ bound to the amyloid-β peptide may be one of the sources of neurodegeneration observed in Alzheimer’s disease. Understanding the structure and function of the copper binding site can assist in the design of effective therapeutics. This paper highlights some of the most significant recent developments in computational modelling studies of the structure of the binding site and reaction mechanisms of reactive oxygen species generation.

scholarly journals Hybrid Bis-Histidine Phenanthroline-Based Ligands to Lessen Aβ-Bound Cu ROS Production: An Illustration of Cu(I) Significance

Molecules ◽  
2021 ◽  
Vol 26 (24) ◽  
pp. 7630
Author(s):  
Marielle Drommi ◽  
Clément Rulmont ◽  
Charlène Esmieu ◽  
Christelle Hureau
Keyword(s):  
Alzheimer’S Disease ◽  
Reactive Oxygen Species ◽  
Alzheimer's Disease ◽  
Copper Complexes ◽  
Amyloid Β ◽  
Reactive Oxygen ◽  
Complete Characterization ◽  
Amyloid Β Peptide ◽  
Oxygen Species ◽  
Hybrid Ligands

We here report the synthesis of three new hybrid ligands built around the phenanthroline scaffold and encompassing two histidine-like moieties: phenHH, phenHGH and H’phenH’, where H correspond to histidine and H’ to histamine. These ligands were designed to capture Cu(I/II) from the amyloid-β peptide and to prevent the formation of reactive oxygen species produced by amyloid-β bound copper in presence of physiological reductant (e.g., ascorbate) and dioxygen. The amyloid-β peptide is a well-known key player in Alzheimer’s disease, a debilitating and devasting neurological disorder the mankind has to fight against. The Cu-Aβ complex does participate in the oxidative stress observed in the disease, due to the redox ability of the Cu(I/II) ions. The complete characterization of the copper complexes made with phenHH, phenHGH and H’phenH’ is reported, along with the ability of ligands to remove Cu from Aβ, and to prevent the formation of reactive oxygen species catalyzed by Cu and Cu-Aβ, including in presence of zinc, the second metal ions important in the etiology of Alzheimer’s disease. The importance of the reduced state of copper, Cu(I), in the prevention and arrest of ROS is mechanistically described with the help of cyclic voltammetry experiments.

Sign in / Sign up

Export Citation Format

Share Document