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  Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization

Dominguez-Meijide, A., Vasili, E., König, A., Cima-Omori, M.-S., Ibáñez de Opakua, A., Leonov, A., et al. (2020). Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization. Scientific Reports, 10: 12827. doi:10.1038/s41598-020-69744-y.

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Dominguez-Meijide, A., Author
Vasili, E., Author
König, A., Author
Cima-Omori, M.-S., Author
Ibáñez de Opakua, A. , Author
Leonov, A.1, Author              
Ryazanov, S.2, Author              
Zweckstetter, M.3, Author              
Griesinger, C.1, Author              
Outeiro, T. F., Author
Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
2Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
3Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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Free keywords: Cell biology; Neuroscience
 Abstract: Parkinson's disease (PD) and Alzheimer's disease (AD) are common neurodegenerative disorders of the elderly and, therefore, affect a growing number of patients worldwide. Both diseases share, as a common hallmark, the accumulation of characteristic protein aggregates, known as Lewy bodies (LB) in PD, and neurofibrillary tangles in AD. LBs are primarily composed of misfolded α-synuclein (aSyn), and neurofibrillary tangles are primarily composed of tau protein. Importantly, upon pathological evaluation, most AD and PD/Lewy body dementia cases exhibit mixed pathology, with the co-occurrence of both LB and neurofibrillary tangles, among other protein inclusions. Recent studies suggest that both aSyn and tau pathology can spread and propagate through neuronal connections. Therefore, it is important to investigate the mechanisms underlying aggregation and propagation of these proteins for the development of novel therapeutic strategies. Here, we assessed the effects of different pharmacological interventions on the aggregation and internalization of tau and aSyn. We found that anle138b and fulvic acid decrease aSyn and tau aggregation, that epigallocatechin gallate decreases aSyn aggregation, and that dynasore reduces tau internalization. Establishing the effects of small molecules with different chemical properties on the aggregation and spreading of aSyn and tau will be important for the development of future therapeutic interventions.

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Language(s): eng - English
 Dates: 2020-07-30
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41598-020-69744-y
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Title: Scientific Reports
Source Genre: Journal
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Pages: - Volume / Issue: 10 Sequence Number: 12827 Start / End Page: - Identifier: -