AHSA2 Inhibitors
AHSA2 inhibitors are a class of compounds that target the ATPase Hsp90 Activating protein 2 (AHSA2), a co-chaperone involved in the Hsp90 chaperone machinery. AHSA2 plays a crucial role in regulating the activity of Hsp90, a heat shock protein that assists in the folding, stabilization, and conformational maturation of a wide array of client proteins. By modulating Hsp90's ATPase activity, AHSA2 influences the chaperoning cycle, affecting the structural and functional integrity of client proteins. AHSA2 binds to the middle domain of Hsp90, enhancing its ATP hydrolysis rate and promoting a conformational state conducive to the progression of the chaperone cycle. Inhibitors targeting AHSA2 interfere with this process, disrupting the delicate balance of Hsp90's activity and its interactions with client proteins.
Chemically, AHSA2 inhibitors are often small molecules designed to bind specifically to the regions of AHSA2 that interact with Hsp90, blocking the facilitation of ATPase activity. These inhibitors may disrupt the protein-protein interactions or allosterically modify the binding affinity of AHSA2 to Hsp90. Their molecular structures are typically optimized to ensure selective binding, stability, and affinity to the AHSA2 protein. Structural studies, including X-ray crystallography and NMR spectroscopy, have been employed to elucidate the precise binding modes of these inhibitors. This has allowed for the rational design of AHSA2 inhibitors that effectively target its function within the chaperone cycle. Research into AHSA2 inhibitors also focuses on understanding the broader implications for protein homeostasis and folding mechanisms, as interference with chaperone systems can result in downstream effects on proteome dynamics and cellular stress responses.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Geldanamycin | 30562-34-6 | sc-200617B sc-200617C sc-200617 sc-200617A | 100 µg 500 µg 1 mg 5 mg | $39.00 $59.00 $104.00 $206.00 | 8 | |
Geldanamycin binds to Hsp90 and inhibits its chaperone activity, which is essential for the proper folding and function of many proteins, including AHSA2. Inhibition of Hsp90 can lead to the destabilization and degradation of AHSA2. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $67.00 $156.00 | 16 | |
17-AAG is a derivative of Geldanamycin and also binds to Hsp90, inhibiting its function. As AHSA2 requires Hsp90 for stability, 17-AAG's action results in the functional inhibition of AHSA2. | ||||||
Radicicol | 12772-57-5 | sc-200620 sc-200620A | 1 mg 5 mg | $92.00 $333.00 | 13 | |
Radicicol binds competitively to the ATP-binding site of Hsp90, thereby inhibiting its activity. Since AHSA2 is a client protein of Hsp90, Radicicol's inhibition of Hsp90 leads to a decrease in AHSA2 activity. | ||||||
17-DMAG | 467214-20-6 | sc-202005 | 1 mg | $205.00 | 8 | |
Alvespimycin, another Hsp90 inhibitor, binds to the N-terminal domain of Hsp90, preventing its association with client proteins like AHSA2. This results in the inhibition of AHSA2 function. | ||||||
Novobiocin | 303-81-1 | sc-362034 sc-362034A | 5 mg 25 mg | $128.00 $380.00 | ||
Novobiocin is an antibiotic that also inhibits the C-terminal ATPase activity of Hsp90. As AHSA2 relies on Hsp90 for conformational support, the inhibition of Hsp90 by Novobiocin reduces AHSA2's activity. | ||||||
Ganetespib | 888216-25-9 | sc-364496 sc-364496A | 10 mg 250 mg | $273.00 $1040.00 | ||
Ganetespib is a potent Hsp90 inhibitor that disrupts the chaperone cycle, leading to the degradation of client proteins including AHSA2, thereby inhibiting its function. | ||||||
AT13387 | 912999-49-6 | sc-364415 sc-364415A | 10 mg 50 mg | $555.00 $1606.00 | ||
Onalespib is an Hsp90 inhibitor that binds to the ATP-binding domain of Hsp90, inhibiting its chaperone function and negatively impacting AHSA2 stability and activity. | ||||||
BIIB 021 | 848695-25-0 | sc-364434 sc-364434A | 5 mg 25 mg | $128.00 $650.00 | ||
BIIB021 is an orally bioavailable Hsp90 inhibitor that binds to the ATP binding domain of Hsp90, leading to the degradation of its client proteins such as AHSA2, and thus inhibiting AHSA2 activity. | ||||||
NVP-AUY922 | 747412-49-3 | sc-364551 sc-364551A sc-364551B sc-364551C sc-364551D sc-364551E | 5 mg 25 mg 100 mg 250 mg 1 g 5 g | $150.00 $263.00 $726.00 $1400.00 $2900.00 $11000.00 | 3 | |
Luminespib is an isoxazole-based Hsp90 inhibitor that disrupts the chaperone function of Hsp90, leading to the degradation of client proteins such as AHSA2, reducing its function. | ||||||
Zerumbone | 471-05-6 | sc-364148 sc-364148A | 10 mg 50 mg | $112.00 $408.00 | ||
Zerumbone has been shown to disrupt the protein-protein interactions of Hsp90 with its co-chaperones, which are necessary for the maturation of client proteins like AHSA2, thereby inhibiting AHSA2's activity. | ||||||