Synucleozid (0.25-1 μM; 24 hours) abrogates cytotoxicity induced by α-synuclein preformed fibrils, which act as seeds and recruit endogenous α-synuclein to aggregate[1]. Synucleozid (0-1 μM; 24 hours) binds to the A bulge near the base of the IRE hairpin, reduced levels of α-synuclein in a dose-dependent manner with an IC50 of 500 nM, and inhibits α-synuclein protein expression in SH-SY5Y neuroblastoma cells[1]. Synucleozid (100 nM-100 μM; 24 hours) binds to 2-AP-labeled and native IRE RNA with similar affinities. It decreases 2-AP emission with an EC50 value of 2.7 μM, recovery of 2-AP emissions is observed as a function of unlabeled SNCA IRE RNA (RNA-0) concentration, affording a competitive Kd of 1.5 μM[1]. Synucleozid (0.25-1 μM; 24 hours) decreases α-synuclein and other proteins that have IREs in their mRNA’s UTR including APP, PrP, Ferritin and TfR as a dose-dependent mannner. All panels is completed in SH-SY5Y cells, except for PrP protein which is assessed in Neuro-2A cells[1]. Cell Viability Assay[1] Cell Line: SH-SY5Y neuroblastoma cells Concentration: 0.25 μM, 0.5 μM, 1 μM Incubation Time: 24 hours Result: Decreased LDH release as a dose-dependent manner. Western Blot Analysis[1] Cell Line: SH-SY5Y neuroblastoma cells Concentration: 0.25 μM; 0.5 μM; 1 μM; Incubation Time: 24 hours Result: Decreased α-synuclein expression as a concentration-dependent manner.
Kinase Assay
Cell Assay
Animal Administration
References
[1]. Zhang P, et al. Translation of the intrinsically disordered protein α-synuclein is inhibited by a small molecule targeting its structured mRNA.Proc Natl Acad Sci U S A. 2020 Jan 21;117(3):1457-1467.
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