Intracellular spatially-targeted chemical chaperones increase native state stability of mutant SOD1 barrel.
SOD1
chemical chaperones
organelle-targeting therapy
osmolytes
protein folding and aggregation
targeted drugs
Journal
Biological chemistry
ISSN: 1437-4315
Titre abrégé: Biol Chem
Pays: Germany
ID NLM: 9700112
Informations de publication
Date de publication:
26 09 2023
26 09 2023
Historique:
received:
30
04
2023
accepted:
25
07
2023
medline:
18
9
2023
pubmed:
9
8
2023
entrez:
9
8
2023
Statut:
epublish
Résumé
Amyotrophic lateral sclerosis (ALS) is a progressive neurological disorder with currently no cure. Central to the cellular dysfunction associated with this fatal proteinopathy is the accumulation of unfolded/misfolded superoxide dismutase 1 (SOD1) in various subcellular locations. The molecular mechanism driving the formation of SOD1 aggregates is not fully understood but numerous studies suggest that aberrant aggregation escalates with folding instability of mutant apoSOD1. Recent advances on combining organelle-targeting therapies with the anti-aggregation capacity of chemical chaperones have successfully reduce the subcellular load of misfolded/aggregated SOD1 as well as their downstream anomalous cellular processes at low concentrations (micromolar range). Nevertheless, if such local aggregate reduction directly correlates with increased folding stability remains to be explored. To fill this gap, we synthesized and tested here the effect of 9 ER-, mitochondria- and lysosome-targeted chemical chaperones on the folding stability of truncated monomeric SOD1 (SOD1
Identifiants
pubmed: 37555646
pii: hsz-2023-0198
doi: 10.1515/hsz-2023-0198
doi:
Substances chimiques
Superoxide Dismutase-1
EC 1.15.1.1
Molecular Chaperones
0
SOD1 protein, human
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
909-930Informations de copyright
© 2023 the author(s), published by De Gruyter, Berlin/Boston.
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