FIGNL2 Inhibitors

Chemical inhibitors of FIGNL2 disrupt the protein's role in DNA repair through various mechanisms. Etoposide, a topoisomerase II inhibitor, creates a barrier for FIGNL2 by inducing DNA strand breaks that the protein typically repairs. Similarly, mitoxantrone and amsacrine also target topoisomerase II, leading to an accumulation of DNA strand breaks and impeding FIGNL2's ability to mediate repair. Teniposide compounds the problem, binding to the topoisomerase II-DNA complex and increasing the number of breaks in the DNA strands. These topoisomerase inhibitors collectively contribute to a surge in damaged DNA that challenges FIGNL2's repair capacity. Doxorubicin and daunorubicin, both intercalating agents, associate with topoisomerase II as well, creating additional breaks in DNA strands that FIGNL2 is tasked to repair. The overload of DNA damage from these agents can overwhelm the repair mechanisms, thus inhibiting the protein's function.

The DNA intercalation method is further employed by idarubicin and epirubicin, which exacerbate DNA damage. Pixantrone continues this trend, adding to the DNA insults that FIGNL2 must address. Actinomycin D's mechanism of binding to the transcription initiation complex and preventing RNA polymerase from progressing also leads to DNA damage that FIGNL2 would typically repair. Mitomycin C introduces an alternative form of DNA lesion through cross-linking, which presents a significant challenge for FIGNL2's role in DNA repair. The cumulative effect of these chemical inhibitors creates a substantial burden on FIGNL2's ability to maintain genomic stability by impeding its essential function in the DNA repair process.