Protein Interactome of Amyloid-β as a Therapeutic Target

The amyloid concept of Alzheimer's disease (AD) assumes the β-amyloid peptide (Aβ) as the main pathogenic factor, which injures neural and other brain cells, causing their malfunction and death. Although Aβ has been documented to exert its cytotoxic effect in a solitary manner, there is much ev...

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Bibliographic Details
Published in:	Pharmaceuticals (Basel, Switzerland) Vol. 16; no. 2; p. 312
Main Authors:	Lazarev, Vladimir F, Dutysheva, Elizaveta A, Kanunikov, Igor E, Guzhova, Irina V, Margulis, Boris A
Format:	Journal Article
Language:	English
Published:	Switzerland MDPI AG 01-02-2023 MDPI
Subjects:	Aggregates Alzheimer's disease Amino acids Amyloid beta-protein amyloid fibrils Analysis Brain Care and treatment chaperones Cytotoxicity Development and progression Extracellular matrix GAPDH Health aspects Heparan sulfate Homeostasis Lipids Neurosciences Neurotoxicity Oxidative stress Peptides Phosphorylation Plasma Protein-protein interactions Proteins protein–protein interaction Review Risk factors Toxicity Transgenic animals α-synuclein Russia Alzheimer’s disease therapeutical agent amyloid fibrils protein–protein interaction tau-protein GAPDH chaperones cytotoxicity α-synuclein
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Summary:	The amyloid concept of Alzheimer's disease (AD) assumes the β-amyloid peptide (Aβ) as the main pathogenic factor, which injures neural and other brain cells, causing their malfunction and death. Although Aβ has been documented to exert its cytotoxic effect in a solitary manner, there is much evidence to claim that its toxicity can be modulated by other proteins. The list of such Aβ co-factors or interactors includes tau, APOE, transthyretin, and others. These molecules interact with the peptide and affect the ability of Aβ to form oligomers or aggregates, modulating its toxicity. Thus, the list of potential substances able to reduce the harmful effects of the peptide should include ones that can prevent the pathogenic interactions by specifically binding Aβ and/or its partners. In the present review, we discuss the data on Aβ-based complexes in AD pathogenesis and on the compounds directly targeting Aβ or the destructors of its complexes with other polypeptides.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 These authors contributed equally to this work.
ISSN:	1424-8247 1424-8247
DOI:	10.3390/ph16020312