DDX19B Inhibitors

Chemical inhibitors of DDX19B target the protein's essential functions, such as ATP hydrolysis and RNA binding, which are critical for its helicase activity involved in nucleocytoplasmic transport of RNA. Novobiocin serves a similar function by binding to the ATPase domain of DDX19B, thereby impeding the necessary conformational changes required for its RNA helicase function. Aurintricarboxylic Acid inhibits DDX19B by obstructing the interaction between the protein and RNA, as it binds to the nucleic acid binding sites of DDX19B, which prevents the protein from performing its RNA-unwinding function. Interference with nucleic acid structures is another strategy employed by inhibitors such as Ethidium Bromide and Berberine; these compounds intercalate with nucleic acids, altering their structure and thus inhibiting DDX19B's ability to bind or unwind its substrate.

Additional chemicals, like Amsacrine and Mitoxantrone, disrupt the function of DDX19B by similar means. By inserting themselves into DNA, they create a distorted nucleic acid structure that DDX19B cannot effectively engage with, thereby hindering its helicase action. Actinomycin D binds to DNA and impedes DNA-dependent RNA synthesis, leading to inhibition of DDX19B by steric hindrance, preventing the protein from interacting with its RNA substrate. Suramin and Heparin inhibit DDX19B through a different mechanism; they bind to the protein and obstruct its interaction with RNA substrates, which is essential for its helicase activity. Oxaliplatin forms DNA adducts and crosslinks that are not easily unwound by DDX19B, leading to the inhibition of the protein's helicase activity. Lastly, Daunorubicin, through its intercalation into DNA, prevents the unwinding action of DDX19B, thus inhibiting the protein's role in the nucleocytoplasmic transport of RNA.