A bifunctional non-natural tetrapeptide modulates amyloid-beta peptide aggregation in the presence of Cu(ii)

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.

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

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.


Polymers ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1051
Author(s):  
Mohamed Abbas

The disorder of Alzheimer’s is marked by progressive pathophysiological neurodegeneration. The amino acid peptides in the amyloid plaques found in the brains of people with Alzheimer’s disease (AD) are known as amyloid-beta (Aβ). Current treatments are not curative, and the effects associated with AD are reduced. Improving treatment results involved the targeting of drugs at optimum therapeutic concentration. Nanotechnology is seen as an unconventional, modern technology that plays a key role in the treatment of Alzheimer’s disease. Using nanoparticles, molecular detection, effective drug targeting, and their combination offer high sensitivity. The aim of this review is to shed light on the function and successful role of nanoparticles to resolve Aβ aggregation and thus to help cure Alzheimer’s disease. The analysis divides these nanoparticles into three categories: polymer, lipid, and gold nanoparticles. A thorough comparison was then made between the nanoparticles, which are used according to their role, properties, and size in the procedure. The nanoparticles can prevent the accumulation of Aβ during the efficient delivery of the drug to the cells to treat Alzheimer’s disease. Furthermore, this comparison demonstrated the ability of these nanoparticles to deal efficiently with Alzheimer’s disease. The role of these nanoparticles varied from delivering the drug to brain cells to dealing with the disease-causing peptide.


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

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