|Molecular Weight||349.4 g/mol|
|Solubility||Soluble in DMSO at 40 mg/mL or ethanol at 25 mg/mL.|
Serine/arginine-rich protein-specific kinases (SRPKs) 1 and 2 phosphorylate and regulate serine/arginine-rich (SR) proteins that bind and regulate mRNA splicing, playing an important role in post-transcriptional regulation (1). The small-molecule SRPIN340 is an SRPK inhibitor that is highly selective for SRPK1 (Ki = 0.89 mM) and SRPK2. SRPK dysregulation can alter SR protein activity and promote expression of splicing isoforms, leading to increased viral infection or tumorigenic processes. Inhibition of SRPK1 and SRPK2 by SRPIN340 reduces SRp75 protein phosphorylation, leading to suppressed Sindbis virus propagation and reduced HIV production (2). Dose-dependent suppression of hepatitis C virus replication by the inhibitor SRPIN340 has been seen in vitro (1). SRPIN340 treatment of leukemia cells triggered early and late events of apoptosis, and reduced myeloid and lymphoid leukemia cell viability (3). Suppression of VEGF by SRPIN340 inhibited choroidal neovascularization formation in a mouse model, suggesting a possible role for SRPIN340 in treating neovascular age-related macular degeneration (4).
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