Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy.
AFM
FTIR
LDH cell toxicity tests
MTT
NMR
S100A9
ThT fluorescence assay
amyloid proteins
fibrils
synuclein
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
17 Jun 2022
17 Jun 2022
Historique:
received:
25
05
2022
revised:
14
06
2022
accepted:
15
06
2022
entrez:
24
6
2022
pubmed:
25
6
2022
medline:
28
6
2022
Statut:
epublish
Résumé
S100A9 is a pro-inflammatory protein that co-aggregates with other proteins in amyloid fibril plaques. S100A9 can influence the aggregation kinetics and amyloid fibril structure of alpha-synuclein (α-syn), which is involved in Parkinson's disease. Currently, there are limited data regarding their cross-interaction and how it influences the aggregation process. In this work, we analyzed this interaction using solution 19F and 2D
Identifiants
pubmed: 35743221
pii: ijms23126781
doi: 10.3390/ijms23126781
pmc: PMC9224231
pii:
doi:
Substances chimiques
Amyloid
0
Calgranulin B
0
alpha-Synuclein
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Latvijas Organiskās Sintēzes Institūts
ID : 1.1.1.2/VIAA/2/18/374
Organisme : Latvijas Organiskās Sintēzes Institūts
ID : 1.1.1.2/VIAA/2/18/379
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