Keratin 80 Inhibitors

Chemical inhibitors of Keratin 80 target the protein's interactions with the cytoskeleton, a crucial component for its function within the cellular structure. Phalloidin, a chemical that stabilizes F-actin, can competitively inhibit the interaction of Keratin 80 with actin, essential for maintaining the cytoskeleton's structure. Withaferin A disrupts intermediate filaments by binding to annexin II, a protein implicated in the organization of Keratin 80, thereby potentially hindering its structural role in the cell. Swinholide A, by severing actin filaments, leads to cytoskeletal disruption, which can inhibit Keratin 80's ability to form proper networks essential for mechanical resilience and cellular integrity. Continuing with the theme of cytoskeletal interference, Cytochalasin D binds to the barbed ends of actin filaments, preventing their polymerization, which can disrupt Keratin 80 interactions with actin, while Jasplakinolide stabilizes actin filaments and inhibits Keratin 80 interaction with the actin cytoskeleton by preventing filament turnover. Latrunculin A's binding to actin monomers prevents their polymerization, which is necessary for Keratin 80 to maintain cellular integrity. Chelidonine and Griseofulvin interact with tubulin, the building block of microtubules, destabilizing and inhibiting microtubule polymerization respectively, which can disrupt Keratin 80's interaction with the cytoskeleton. Similarly, Colchicine and Vinblastine inhibit microtubule assembly, which can inhibit Keratin 80's ability to interact with the cytoskeleton for cell structure, and Nocodazole disrupts microtubule dynamics, which may inhibit the proper organization and function of Keratin 80 in cells. Paclitaxel, on the other hand, stabilizes microtubules and thus potentially inhibits Keratin 80's interaction with the cytoskeleton by impairing dynamics, offering a unique approach to hindering Keratin 80's functional capacity within the cytoskeletal framework.