scholarly journals Modification of Amyloid-beta Peptide Aggregation via Photoactivation of Strained Ru(II) Polypyridyl Complexes

2021 ◽  
Author(s):  
Janaina Bataglioli ◽  
Luiza M. F. Gomes ◽  
Camille Maunoir ◽  
Jason Smith ◽  
Houston D. Cole ◽  
...  

Alzheimer’s disease (AD) is a chronic neurodegenerative disorder characterized by progressive and irreversible damage to the brain. One of the hallmarks of the disease is the presence of both soluble...

RSC Advances ◽  
2017 ◽  
Vol 7 (50) ◽  
pp. 31714-31724 ◽  
Author(s):  
Antonella Battisti ◽  
Antonio Palumbo Piccionello ◽  
Antonella Sgarbossa ◽  
Silvia Vilasi ◽  
Caterina Ricci ◽  
...  

This study suggests new concepts and potential difficulties in the design of novel drugs against diverse amyloidoses, including Alzheimer’s disease.


2015 ◽  
Vol 11 (7S_Part_7) ◽  
pp. P352-P353 ◽  
Author(s):  
Olivia Berthoumieu ◽  
Peter Faller ◽  
Andrew J. Doig ◽  
Philippe Derreumaux

Metallomics ◽  
2014 ◽  
Vol 6 (12) ◽  
pp. 2189-2192 ◽  
Author(s):  
Maripaz Márquez ◽  
Luis M. Blancas-Mejía ◽  
Adriana Campos ◽  
Luis Rojas ◽  
Gilberto Castañeda-Hernández ◽  
...  

A novel bifunctional non-natural tetrapeptide, Met-Asp-d-Trp-Aib, is capable of binding copper, competing with amyloid-beta peptide (Aβ) for Cu(ii), and modulating Aβ aggregation. The study of this tetrapeptide provides further insights into the role of Cu(ii) in the Aβ aggregation pathway, and into the design of compounds with therapeutic potential for Alzheimer's disease.


2019 ◽  
Vol 10 (6) ◽  
pp. 1634-1643 ◽  
Author(s):  
Luiza M. F. Gomes ◽  
Atif Mahammed ◽  
Kathleen E. Prosser ◽  
Jason R. Smith ◽  
Michael A. Silverman ◽  
...  

An Fe corrole is shown to bind to the amyloid-beta peptide and limit reactive oxygen species generation and peptide aggregation of relevance to Alzheimer's disease.


2011 ◽  
Vol 2011 ◽  
pp. 1-13 ◽  
Author(s):  
Mallory Gough ◽  
Catherine Parr-Sturgess ◽  
Edward Parkin

Alzheimer's disease is a neurodegenerative condition characterized by an accumulation of toxic amyloid beta- (A-)peptides in the brain causing progressive neuronal death. A-peptides are produced by aspartyl proteinase-mediated cleavage of the larger amyloid precursor protein (APP). In contrast to this detrimental “amyloidogenic” form of proteolysis, a range of zinc metalloproteinases can process APP via an alternative “nonamyloidogenic” pathway in which the protein is cleaved within its A region thereby precluding the formation of intact A-peptides. In addition, other members of the zinc metalloproteinase family can degrade preformed A-peptides. As such, the zinc metalloproteinases, collectively, are key to downregulating A generation and enhancing its degradation. It is the role of zinc metalloproteinases in this “positive side of proteolysis in Alzheimer's disease” that is discussed in the current paper.


2004 ◽  
Vol 91 (3) ◽  
pp. 648-656 ◽  
Author(s):  
Yuanbin Liu ◽  
Richard Dargusch ◽  
Cindy Banh ◽  
Carol A. Miller ◽  
David Schubert

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