Date published: 2025-12-19

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ProSAPiP1 Inhibitors

ProSAPiP1 inhibitors represent a class of compounds that specifically target the Proline-rich synapse-associated protein 1 (ProSAPiP1), a scaffolding protein located predominantly in synaptic junctions. ProSAPiP1 plays a significant role in the structural organization and functionality of postsynaptic density (PSD), particularly by interacting with other synaptic proteins like Shank proteins, which are crucial for synaptic signaling and plasticity. Inhibitors of ProSAPiP1 are designed to disrupt these protein-protein interactions, thereby modulating the architecture and dynamics of the postsynaptic compartment. This can lead to changes in synaptic strength and the plastic responses of neurons, particularly influencing the molecular machinery that governs synaptic transmission and signal transduction pathways. The selective inhibition of ProSAPiP1 can serve as a molecular tool to dissect the contributions of this protein to synaptic function and to better understand the regulation of PSD components.

These inhibitors offer insights into the intricate molecular mechanisms that govern synaptic homeostasis and plasticity. By controlling the interactions of ProSAPiP1 within the synapse, these inhibitors help researchers explore how synaptic architecture is remodeled during processes such as learning, memory formation, and neuronal communication. ProSAPiP1's interaction network within the PSD is complex, involving a variety of cytoskeletal and signaling proteins, and its inhibition has downstream effects on other synaptic scaffolding complexes, potentially altering excitatory and inhibitory balance within neural circuits. The ability to fine-tune these molecular interactions with inhibitors not only allows for the exploration of the fundamental principles of synaptic biology but also aids in uncovering novel pathways that underlie the synaptic modifications linked to broader neurobiological processes.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

KN-93

139298-40-1sc-202199
1 mg
$178.00
25
(1)

Specific inhibitor of calcium/calmodulin-dependent protein kinase II (CaMKII). Inhibiting CaMKII activity may disrupt ProSAPiP1-related signaling pathways.

Jasplakinolide

102396-24-7sc-202191
sc-202191A
50 µg
100 µg
$180.00
$299.00
59
(1)

Natural compound that stabilizes actin filaments. Potential indirect inhibitor of ProSAPiP1 by influencing actin dynamics at synapses.

Cytochalasin D

22144-77-0sc-201442
sc-201442A
1 mg
5 mg
$145.00
$442.00
64
(4)

Disrupts actin polymerization by binding to the barbed end of actin filaments. May indirectly affect ProSAPiP1 by altering actin cytoskeleton organization.

(±)-Blebbistatin

674289-55-5sc-203532B
sc-203532
sc-203532A
sc-203532C
sc-203532D
5 mg
10 mg
25 mg
50 mg
100 mg
$179.00
$307.00
$455.00
$924.00
$1689.00
7
(1)

Inhibitor of myosin II ATPase activity. Potential indirect inhibitor of ProSAPiP1 through modulation of actin-myosin interactions.

KN-62

127191-97-3sc-3560
1 mg
$133.00
20
(2)

Calmodulin-dependent protein kinase II (CaMKII) inhibitor. May disrupt ProSAPiP1-related signaling pathways by inhibiting CaMKII activity.

Latrunculin A, Latrunculia magnifica

76343-93-6sc-202691
sc-202691B
100 µg
500 µg
$260.00
$799.00
36
(2)

Toxin found in marine sponges that disrupts actin polymerization. Potential indirect inhibitor of ProSAPiP1 by affecting actin cytoskeleton dynamics.

Y-27632, free base

146986-50-7sc-3536
sc-3536A
5 mg
50 mg
$182.00
$693.00
88
(1)

Inhibitor of Rho-associated protein kinase (ROCK). May indirectly impact ProSAPiP1 through modulation of actin cytoskeleton and synaptic organization.

Phalloidin

17466-45-4sc-202763
1 mg
$229.00
33
(1)

Toxin that stabilizes actin filaments. Potential indirect inhibitor of ProSAPiP1 by influencing actin dynamics and synaptic organization.

ML-7 hydrochloride

110448-33-4sc-200557
sc-200557A
10 mg
50 mg
$89.00
$262.00
13
(1)

Inhibitor of myosin light chain kinase (MLCK). Potential indirect inhibitor of ProSAPiP1 through modulation of actin-myosin interactions.