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A direct interaction between mitochondrial proteins and amyloid-β peptide and its significance for the development and treatment of Alzheimer’s disease

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Benek_CMC_2015_corrected.pdf (1.212Mb)
Date
2015
Author
Benek, Ondrej
Aitken, Laura
Hroch, Lukas
Kuca, Kamil
Gunn-Moore, Frank J
Musilek, Kamil
Funder
Alzheimer's Society
Scottish Funding Council
Grant ID
188 PG-2012-172
MSDPD03
Keywords
Alzheimer's disease
Amyloid-beta peptide
Drug target
Enzyme inhibition
Mitochondria
Pharmacotherapy
QH301 Biology
I-PW
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Abstract
The amyloid-β peptide (Aβ) has been associated with Alzheimer’s disease (AD) for decades. The original amyloid cascade hypothesis declared that the insoluble extracellular plaques were responsible for Aβ toxicity. Later, this hypothesis has been updated and soluble intracellular Aβ forms and their effects within the cell have come into focus. Mitochondrial dysfunction plays an important role in the pathophysiology of AD. Aβ was detected inside mitochondria and several mitochondrial proteins were found to interact directly with Aβ. Such interactions can affect a protein’s function and cause damage to the mitochondria and finally to the whole cell. This review summarizes the current knowledge of mitochondrial proteins directly interacting with Aβ and discusses their significance for the development of therapeutics in the treatment of AD.
Citation
Benek , O , Aitken , L , Hroch , L , Kuca , K , Gunn-Moore , F J & Musilek , K 2015 , ' A direct interaction between mitochondrial proteins and amyloid-β peptide and its significance for the development and treatment of Alzheimer’s disease ' , Current Medicinal Chemistry , vol. 22 , no. 9 , pp. 1056-1085 . https://doi.org/10.2174/0929867322666150114163051
Publication
Current Medicinal Chemistry
Status
Peer reviewed
DOI
https://doi.org/10.2174/0929867322666150114163051
ISSN
0929-8673
Type
Journal article
Rights
© 2015. Bentham Science Publishers. This is the author’s version of a work that was accepted for publication in Current Medicinal Chemistry. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Current Medicinal Chemistry, 2015 DOI http://dx.doi.org/10.2174/0929867322666150114163051
Description
This work was supported by the Ministry of Education, Youth and Sports CZ (no. LD14009, no. SV/FVZ201201, no. SVV260062), COST CM1103, MH CZ - DRO (UHHK, 00179906), The Alzheimer’s Society, The Barcopel Foundation and the MSD Scottish Life Sciences fund.
Collections
  • University of St Andrews Research
URI
http://hdl.handle.net/10023/8102

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