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• W2023373550 abstract "Nitric oxide (NO) regulates multiple biological processes. To use NO as a potential therapeutic substance, a more selective modulation of individual NO targets is desirable. Here, we tested whether peptide conjugation of the dinitrosyl–iron complex (DNIC), a potent NO donor, confers targeted NO delivery. As target, we used the protease 2A of Coxsackie-B-viruses (2Apro), which can cause dilated cardiomyopathy. Through S-nitrosylation, NO inhibits this protease, which is essential for viral replication. The tetrapeptide Leu-Ser-Thr-Cys (LSTC) (based on the 2Apro substrate recognition motif) and DNIC generated LSTC–DNIC in vitro by S-nitrosylation as evidenced by reverse-phase chromatography. In vitro, LSTC–DNIC (IC50 510 nM) dose-dependently inhibited purified 2Apro 4.7-fold more effectively than DNIC (IC50 2.4 μM), whereas LSTC alone had no effect. In intact cells, expression of Coxsackievirus protease 2A by transient transfection led to eIF4G-I-cleavage. LSTC–DNIC (IC50 23 μM) dose-dependently inhibited eIF4G cleavage in 2Apro-transfected cells 3.8-fold more effectively than DNIC (IC50 88 μM). To test the specificity of the DNIC-conjugated LSTC peptide part, we investigated its influence on Caspase-3, a known target for S-nitrosylation. LSTC–DNIC and DNIC inhibited purified Caspase-3 in vitro (IC50 3.7 μM) and in intact cells similarly. LSTC conjugation of DNIC enhances its fidelity for inhibition of 2Aproin vitro and intracellularly. Peptide–DNIC may be useful to selectively modulate cellular processes by NO, i.e., to enhance its antiviral properties." @default.
• W2023373550 created "2016-06-24" @default.
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• W2023373550 date "2002-05-01" @default.
• W2023373550 modified "2023-09-30" @default.
• W2023373550 title "Selective Delivery of Nitric Oxide to a Cellular Target: A Pseudosubstrate-Coupled Dinitrosyl–Iron Complex Inhibits the Enteroviral Protease 2A" @default.
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• W2023373550 doi "https://doi.org/10.1006/niox.2001.0413" @default.
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