Date published: 2026-4-1

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α-Adaptin Inhibitors

α-Adaptin inhibitors belong to a niche class of molecules that target the protein α-adaptin, a pivotal component of the adaptor protein complex AP-2. AP-2 is integral to the endocytosis process, a mechanism through which cells internalize molecules from their exterior environment by engulfing them in vesicles. This process is crucial for numerous cellular functions, from nutrient uptake to signal regulation. α-Adaptin plays a role in connecting the membrane with the clathrin lattice during clathrin-mediated endocytosis, acting as a linchpin for efficient vesicle formation.

The very architecture of α-adaptin, with its multifaceted domains, makes it a prime target for inhibitors. These inhibitors are typically designed to bind specifically to the active or interaction sites of α-adaptin, thereby hindering its interaction with other proteins or molecules, and in turn, disrupting the endocytosis process. The potency and specificity of these inhibitors are often gauged based on their ability to block or attenuate this protein-protein interaction. The structural diversity of α-adaptin inhibitors ranges from small organic molecules to peptide mimetics, each tailored to target specific sites or domains. Understanding the intricacies of α-adaptin's structure and function is paramount for the design of efficient inhibitors. By tweaking the interactions between α-adaptin and its various partners, these inhibitors provide a toolset for researchers aiming to dissect the nuances of endocytic processes at a molecular level.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Dynamin Inhibitor I, Dynasore

304448-55-3sc-202592
10 mg
$89.00
44
(2)

A non-competitive inhibitor of the GTPase activity of dynamin. Dynamin is involved in the scission of clathrin-coated vesicles from the membrane. By inhibiting dynamin, Dynasore could indirectly affect α-Adaptin's function in the formation and maturation of clathrin-coated pits.

Pitstop 2

1419320-73-2sc-507418
10 mg
$360.00
(0)

A compound that inhibits clathrin by preventing the terminal domain of clathrin from binding to lipids and other adaptors. By preventing clathrin binding, it could indirectly affect the recruitment and function of α-Adaptin, which is part of the AP-2 complex that interacts with clathrin.

Chlorpromazine

50-53-3sc-357313
sc-357313A
5 g
25 g
$61.00
$110.00
21
(1)

An antipsychotic drug. CPZ is known to inhibit clathrin-mediated endocytosis, possibly by disrupting the assembly of clathrin-coated pits. This could affect α-Adaptin's function in the process.

Dansylcadaverine

10121-91-2sc-214851
sc-214851A
sc-214851B
100 mg
250 mg
1 g
$52.00
$89.00
$240.00
4
(1)

Used as a tracer for autophagic vacuoles but can also inhibit clathrin-mediated endocytosis. The exact mechanism by which MDC inhibits clathrin-mediated endocytosis is unclear, but it might affect the assembly or function of clathrin-coated pits, thus affecting α-Adaptin.

Sucrose

57-50-1sc-204311
sc-204311B
sc-204311C
sc-204311A
0.5 kg
50 kg
100 kg
5 kg
$58.00
$2000.00
$3500.00
$250.00
6
(1)

A common sugar. In high concentrations, sucrose can inhibit the formation of clathrin-coated pits, potentially affecting α-Adaptin's role.

Latrunculin A, Latrunculia magnifica

76343-93-6sc-202691
sc-202691B
100 µg
500 µg
$265.00
$815.00
36
(2)

Actin-disrupting agents. Given the role of actin in clathrin-mediated endocytosis, disrupting actin can affect the maturation and scission of clathrin-coated vesicles, potentially affecting α-Adaptin.

Nocodazole

31430-18-9sc-3518B
sc-3518
sc-3518C
sc-3518A
5 mg
10 mg
25 mg
50 mg
$59.00
$85.00
$143.00
$247.00
38
(2)

A microtubule-disrupting agent. Microtubules play roles in transporting vesicles. Disrupting microtubules might indirectly affect clathrin-mediated endocytosis and α-Adaptin's function.

Cytochalasin D

22144-77-0sc-201442
sc-201442A
1 mg
5 mg
$165.00
$486.00
64
(4)

Another actin-disrupting agent. Like latrunculins, by disrupting actin, Cytochalasin D can affect the clathrin-mediated endocytosis process, potentially impacting α-Adaptin.