PSD Inhibitors
PSD inhibitors pertain to a class of chemical compounds that target the Post-synaptic density (PSD) within neuronal cells, specifically at the synapses where the communication between neurons takes place. The PSD is a specialized region within the neuron, rich in proteins and functioning as a network that manages synaptic signaling and plasticity. The complexity of the PSD is attributed to its composition of receptors, ion channels, enzymes, and scaffolding proteins, all of which work in concert to regulate synaptic strength and homeostasis. PSD inhibitors interfere with the normal function of these components, thereby modulating the biochemical pathways within the PSD. Their mode of action typically involves the inhibition of specific enzymes or the alteration of the structural integrity of the scaffold proteins, which can lead to changes in synaptic transmission dynamics.
These inhibitors have generated interest in the scientific community due to their unique mechanism of action, which allows for the modulation of synaptic activity without directly affecting neurotransmitter levels or receptor activity. The intricate nature of PSD function means that PSD inhibitors must demonstrate a high degree of specificity to ensure they target the intended components within the dense network of proteins. The study of these compounds often involves a multi-disciplinary approach, encompassing biochemistry, molecular biology, and neurophysiology to unravel the complex interactions within the PSD. By altering the protein-protein interactions or the enzymatic activities within the PSD, these inhibitors are able to influence the downstream signaling pathways that are crucial for synaptic plasticity and stability. Research into the detailed mechanisms of PSD inhibitors continues to provide insights into the sophisticated molecular machinery that underpins synaptic function and regulation.
Items 1 to 10 of 12 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Phalloidin | 17466-45-4 | sc-202763 | 1 mg | $234.00 | 33 | |
Phalloidin binds to actin filaments, stabilizing them and preventing their disassembly, which is crucial for maintaining dendritic spine structure. PSD relies on a well-organized actin cytoskeleton for its localization and stability in postsynaptic densities. By stabilizing actin filaments, phalloidin can indirectly inhibit the dynamic rearrangement of the PSD, affecting its functionality. | ||||||
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 and prevents their polymerization, leading to the disassembly of actin filaments. Since PSD requires an intact actin cytoskeleton for its structure and synaptic signaling, the disruption of the cytoskeleton by Latrunculin A indirectly decreases PSD stability and function. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $165.00 $486.00 | 64 | |
Cytochalasin D inhibits actin polymerization by capping the fast-growing end of actin filaments, leading to depolymerization. The presence of a stable actin network is vital for PSD integrity; therefore, Cytochalasin D's action compromises the PSD's structural support and signaling capabilities. | ||||||
CK 666 | 442633-00-3 | sc-361151 sc-361151A | 10 mg 50 mg | $321.00 $1040.00 | 5 | |
CK-666 is an inhibitor of the Arp2/3 complex, which is involved in the nucleation of new actin filaments. Inhibition of the Arp2/3 complex by CK-666 disrupts actin polymerization required for the maintenance of dendritic spines where PSD is localized, thereby indirectly impacting PSD function. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $184.00 $305.00 | 59 | |
Jasplakinolide stabilizes actin filaments and also promotes actin polymerization. By locking actin in a polymerized state, it disrupts the dynamic equilibrium necessary for synaptic plasticity, which is essential for the functional modulation of PSD within the synapse. | ||||||
Nocodazole | 31430-18-9 | sc-3518B sc-3518 sc-3518C sc-3518A | 5 mg 10 mg 25 mg 50 mg | $59.00 $85.00 $143.00 $247.00 | 38 | |
Nocodazole disrupts microtubule networks by inhibiting their polymerization. Microtubules are important for the trafficking of synaptic vesicles and proteins to the synapse, including components of the PSD. The disruption of microtubules by Nocodazole can lead to a decrease in PSD components at the synaptic site, indirectly affecting its activity. | ||||||
Colchicine | 64-86-8 | sc-203005 sc-203005A sc-203005B sc-203005C sc-203005D sc-203005E | 1 g 5 g 50 g 100 g 500 g 1 kg | $100.00 $321.00 $2289.00 $4484.00 $18207.00 $34749.00 | 3 | |
Colchicine binds to tubulin, inhibiting microtubule polymerization and leading to microtubule depolymerization. This action can impair the delivery of essential components and signaling molecules to the PSD, thus indirectly diminishing its structural integrity and signaling function. | ||||||
(±)-Blebbistatin | 674289-55-5 | sc-203532B sc-203532 sc-203532A sc-203532C sc-203532D | 5 mg 10 mg 25 mg 50 mg 100 mg | $183.00 $313.00 $464.00 $942.00 $1723.00 | 7 | |
Blebbistatin is an inhibitor of myosin II ATPase activity, which is required for actin-myosin contractility. Since actin-myosin interactions are important for spine morphology and thus for the stabilization of PSD, Blebbistatin indirectly affects the proper localization and function of PSD. | ||||||
ML-7 hydrochloride | 110448-33-4 | sc-200557 sc-200557A | 10 mg 50 mg | $91.00 $267.00 | 13 | |
ML-7 is an inhibitor of myosin light chain kinase (MLCK), which phosphorylates myosin light chains to promote actin-myosin interactions. Inhibition of MLCK by ML-7 results in decreased actin-myosin contractility, thereby affecting dendritic spine structure and indirectly influencing PSD functionality. | ||||||
Wiskostatin | 253449-04-6 | sc-204399 sc-204399A sc-204399B sc-204399C | 1 mg 5 mg 25 mg 50 mg | $49.00 $124.00 $441.00 $828.00 | 4 | |
Wiskostatin is a selective inhibitor of the N-WASP, which activates the Arp2/3 complex in actin branching and polymerization. By inhibiting N-WASP, Wiskostatin indirectly disrupts the actin cytoskeleton dynamics necessary for maintaining the structure of dendritic spines and the positioning of PSD. | ||||||