ZNF598 Inhibitors

TPEN, an efficient zinc chelator, sequesters zinc away from ZNF213, likely leading to a loss of its structural integrity. Similarly, Clioquinol, an antimicrobial with zinc chelating properties, may destabilize the zinc finger motifs, which are pivotal for the protein's DNA-binding ability. Pyrithione Zinc, another zinc-binding compound, is used for its antibacterial and antifungal properties and shares this mode of action, potentially altering the three-dimensional structure of ZNF213. Beyond chelation, some compounds target specific amino acid residues. Phenylarsine Oxide, for example, binds to vicinal thiol groups, often found in the cysteine-rich regions of zinc finger domains, which could lead to conformational changes in ZNF213, thereby affecting its function. Dithizone, a sulfur-containing chelator, operates similarly, potentially disrupting zinc coordination in the protein's active sites.

EDTA, a ubiquitous chelating agent, can complex with the zinc ions necessary for the zinc finger domains' formation, while 1,10-Phenanthroline, an organic chelator, could bind to the zinc ions in ZNF213, impeding its ability to interact with DNA. Both act by possibly stripping away the essential zinc ions from the protein, leading to a loss of functional conformation. Heavy metals such as Cadmium Chloride can replace zinc in the zinc finger domains, which may result in incorrect protein folding and likely a subsequent loss of function. Diethyldithiocarbamate, another chelator, may contribute to this disruption by binding zinc ions, a critical structural component of ZNF213. The flavonoid Quercetin is known for its ability to modulate protein function and interactions. Although not a chelator, it may affect ZNF213's role in transcription regulation by altering its interactions within the larger protein complex. Aurintricarboxylic Acid, known to inhibit interactions between proteins and nucleic acids, can disrupt the binding of ZNF213 to DNA, thus impeding its regulatory function.