Synucleozid-2.0

Synucleozid-2.0 selectively binds to the A bulge and its closed base pairs of SNCA IRE RNA, with a competitive K_d of 1.8 µM and an EC₅₀ of 2.9 µM in fluorescence-based assays^[1].
Synucleozid-2.0 (0.1-2 µM; 48 h) dose-dependently inhibits the translation of α-synuclein in SH-SY5Y cells with an IC₅₀ of approximately 2 µM, but exerts no effect on the translation of ferritin, TfR or APP^[1].
Synucleozid-2.0 (0.1-2 µM; 48 h) dose-dependently inhibits the translation driven by the internal ribosome entry site (IRE) of SNCA in HeLa cells in luciferase reporter assays, whereas it has no effect on reporter genes lacking the SNCA 5' UTR^[1].
Synucleozid-2.0 (0.5-10 µM; 48 h) exerts dose-dependent cytoprotective effects on SH-SY5Y cells against α-synuclein PFF-induced toxicity, with an EC₅₀ of 13 µM^[1].
Synucleozid-2.0 (0.5-10 µM; 48 h) protects SNCA mRNA in SH-SY5Y cells from RNase H cleavage in a dose-dependent manner by binding to the A-bulge region targeted by Gapmer-1, but has no effect on gapmer-mediated cleavage targeting non-overlapping regions^[1].
Synucleozid-2.0 (0-20 µM; 16 h) competes with Syn-ChemCLIP for binding to the same site on SNCA mRNA in SH-SY5Y cells^[1].
Synucleozid-2.0 inhibits the translation of α-synuclein in SH-SY5Y cells by blocking the formation of preinitiation complex and preventing ribosome loading onto SNCA mRNA^[1].
Synucleozid-2.0 (2 µM; 48 h) reduces α-synuclein levels by approximately 50% in both control and SNCA triplication patient-derived human dopaminergic neurons, without altering SNCA mRNA levels^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.