CapZ-α3 Inhibitors
Chemical inhibitors of CapZ-α3 disrupt its function by interfering with the dynamics of actin filament assembly and disassembly. Latrunculin A, Cytochalasin D, and Cytochalasin B operate by directly blocking the polymerization process at the monomer level or the barbed ends of the actin filaments. Latrunculin A binds to actin monomers and prevents them from polymerizing, thereby eliminating the substrate that CapZ-α3 requires to cap. Similarly, Cytochalasin D and Cytochalasin B hinder CapZ-α3's ability to stabilize actin filaments by binding to the barbed ends, preventing further addition of actin monomers. Swinholide A and Mycalolide B exert their effects by severing actin filaments and sequestering actin monomers respectively. This reduction in the number of intact actin filaments leaves CapZ-α3 with fewer targets for its capping activity.
Other inhibitors such as Phalloidin, Rhodamine phalloidin, Jasplakinolide, Misakinolide A, and Chondramide modulate the stability of actin filaments. Phalloidin and Rhodamine phalloidin increase filament rigidity by binding tightly and preventing depolymerization, which is necessary for the dynamic action of CapZ-α3. Jasplakinolide and Misakinolide A similarly stabilize and nucleate filaments, thus reducing the availability of free barbed ends required for CapZ-α3's function. Chondramide's binding to actin filaments inhibits their dynamics, which are necessary for the proper functioning of CapZ-α3. Furthermore, Tropomyosin competes with CapZ-α3 for binding sites along the length of actin filaments, effectively reducing the opportunity for CapZ-α3 to cap the growing filaments. Lastly, while the specific mechanism in CapZ-α3 is not detailed, Beryllium fluoride can bind to nucleotide-binding proteins, which may interfere with any ATPase activity associated with CapZ-α3, thereby inhibiting its function. Each of these chemicals, through their unique interactions with actin or actin-associated processes, can disrupt the stabilizing role CapZ-α3 plays in cellular actin dynamics.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $265.00 $815.00 | 36 | |
Latrunculin A binds to actin monomers, preventing their polymerization. Since CapZ-α3 is involved in capping the barbed ends of actin filaments, the prevention of actin polymerization by Latrunculin A would result in the functional inhibition of CapZ-α3 due to the lack of substrate for capping. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $165.00 $486.00 | 64 | |
Cytochalasin D disrupts actin filaments by binding to the barbed ends and preventing elongation. This directly inhibits CapZ-α3 by removing the primary structure it caps, effectively inhibiting its function of stabilizing actin filaments. | ||||||
Swinholide A, Theonella swinhoei | 95927-67-6 | sc-205914 | 10 µg | $135.00 | ||
Swinholide A severs actin filaments and prevents their reannealing. As CapZ-α3 functions to cap the growing ends of actin filaments, the severing action of Swinholide A reduces the available actin filaments for CapZ-α3 to act upon, thus functionally inhibiting it. | ||||||
Phalloidin | 17466-45-4 | sc-202763 | 1 mg | $234.00 | 33 | |
Phalloidin stabilizes actin filaments and increases their rigidity. This stabilization inhibits the dynamic function of CapZ-α3 which requires the ability to bind to and dissociate from the fast-growing ends of actin filaments, leading to functional inhibition of CapZ-α3. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $184.00 $305.00 | 59 | |
Jasplakinolide stabilizes and nucleates filaments, and by doing so, it reduces the number of free barbed ends for CapZ-α3 to interact with, thus inhibiting the protein's function in actin filament dynamics. | ||||||