DDX10 Inhibitors

Chemical inhibitors of DDX10 utilize diverse mechanisms to inhibit the helicase activity of this protein. Novobiocin targets the ATPase domain of DDX10, obstructing ATP binding and subsequent helicase activity. Suramin, by interacting with nucleotides and nucleic acids, can inhibit DDX10 by disrupting the enzyme's ability to hydrolyze ATP. Aurintricarboxylic Acid inhibits the interaction between DDX10 and its RNA substrate by binding to the nucleic acid binding sites on DDX10, effectively incapacitating the protein's functional interaction with RNA.

Ethidium Bromide, Berberine, Amsacrine, Daunorubicin, Mitoxantrone, and Actinomycin D all act by interfering with the nucleic acids that DDX10 is meant to engage with. Ethidium Bromide and Berberine intercalate into nucleic acids and alter the structure of RNA or DNA, which hinders DDX10 from binding or unwinding its substrate. This structural alteration of the nucleic acids by intercalating agents presents a barrier to DDX10's helicase activity. Oxaliplatin forms DNA adducts, creating crosslinks within the DNA that are insurmountable by the helicase function of DDX10, thus inhibiting its activity. Actinomycin D binds to DNA and blocks the transcription and interaction sites, making them inaccessible to DDX10, precluding the unwinding action of the helicase. Heparin, though primarily known for its anticoagulant properties, also possesses the ability to bind to proteins that interact with nucleic acids; it can bind to DDX10 and sterically hinder the protein from engaging with its nucleic acid substrates, thus inhibiting the helicase activity.