Cationic Carbosilane Dendrimers Prevent Abnormal α-Synuclein Accumulation in Parkinson's Disease Patient-Specific Dopamine Neurons.
Journal
Biomacromolecules
ISSN: 1526-4602
Titre abrégé: Biomacromolecules
Pays: United States
ID NLM: 100892849
Informations de publication
Date de publication:
08 11 2021
08 11 2021
Historique:
pubmed:
7
10
2021
medline:
16
11
2021
entrez:
6
10
2021
Statut:
ppublish
Résumé
Accumulation of misfolded α-synuclein (α-syn) is a hallmark of Parkinson's disease (PD) thought to play important roles in the pathophysiology of the disease. Dendritic systems, able to modulate the folding of proteins, have emerged as promising new therapeutic strategies for PD treatment. Dendrimers have been shown to be effective at inhibiting α-syn aggregation in cell-free systems and in cell lines. Here, we set out to investigate the effects of dendrimers on endogenous α-syn accumulation in disease-relevant cell types from PD patients. For this purpose, we chose cationic carbosilane dendrimers of bow-tie topology based on their performance at inhibiting α-syn aggregation
Identifiants
pubmed: 34613701
doi: 10.1021/acs.biomac.1c00884
pmc: PMC8906628
doi:
Substances chimiques
Dendrimers
0
SNCA protein, human
0
Silanes
0
alpha-Synuclein
0
carbosilane
0
LRRK2 protein, human
EC 2.7.11.1
Leucine-Rich Repeat Serine-Threonine Protein Kinase-2
EC 2.7.11.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4582-4591Subventions
Organisme : NIMHD NIH HHS
ID : L60 MD003733
Pays : United States
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