The class of VAMP-1 inhibitors comprises a diverse array of compounds designed to directly or indirectly modulate the function of Vesicle-Associated Membrane Protein 1 (VAMP-1), a critical component of the SNARE complex involved in synaptic vesicle exocytosis. The intricate molecular machinery governing neurotransmitter release underscores the significance of identifying specific inhibitors to elucidate the regulatory mechanisms at play. Tetanus Toxin Fragment C and Botulinum Toxin Type A represent two potent neurotoxins that selectively target VAMP-1. Through proteolytic cleavage, these toxins disrupt SNARE complex assembly, preventing the fusion of synaptic vesicles with the cell membrane and thereby inhibiting neurotransmitter release. Their precise mechanisms of action highlight the role of VAMP-1 in the finely tuned process of synaptic vesicle exocytosis.
Furthermore, the chemical class includes synthetic compounds like Exo2, SecinH3, and Dantrolene, each targeting different aspects of the regulatory network. Exo2 interferes with SNARE complex assembly, SecinH3 indirectly modulates VAMP-1 through small GTPase inhibition, and Dantrolene impacts calcium dynamics, indirectly affecting VAMP-1 function. These compounds provide valuable tools for researchers investigating the complex interplay of cellular processes regulating neurotransmitter release. Additionally, PEGylated Nanoparticles, N-Butylidenephthalide, LDV Peptide, and Nocodazole contribute to the class, offering innovative approaches to VAMP-1 modulation. PEGylated Nanoparticles disrupt SNARE complex assembly through nanotechnological engineering, while N-Butylidenephthalide and LDV Peptide provide insights into natural and synthetic compounds targeting VAMP-1. Nocodazole, by disrupting microtubule dynamics, indirectly influences VAMP-1 function, adding a pharmacological dimension to the class. In summary, the chemical class of VAMP-1 inhibitors encompasses a spectrum of compounds that, through diverse mechanisms, shed light on the intricate regulation of synaptic vesicle exocytosis.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
N-Ethylmaleimide | 128-53-0 | sc-202719A sc-202719 sc-202719B sc-202719C sc-202719D | 1 g 5 g 25 g 100 g 250 g | $22.00 $69.00 $214.00 $796.00 $1918.00 | 19 | |
N-Ethylmaleimide (NEM) is a thiol-reactive compound that inhibits VAMP-1 indirectly by blocking disulfide bond formation critical for SNARE complex assembly. By modifying cysteine residues, NEM disrupts the formation of functional SNARE complexes, hindering vesicle fusion and neurotransmitter release. Its action on the thiol groups of VAMP-1 provides a molecular basis for its inhibitory effects. | ||||||
Exo2 | 304684-77-3 | sc-215011 sc-215011A | 5 mg 25 mg | $89.00 $288.00 | 1 | |
Exo2 is a synthetic compound designed to inhibit VAMP-1 by interfering with SNARE complex assembly. By targeting the interaction between VAMP-1 and other SNARE proteins, Exo2 disrupts the fusion of synaptic vesicles with the cell membrane, leading to the inhibition of neurotransmitter release. Its specific mechanism of action highlights its potential as a pharmacological tool for studying synaptic vesicle exocytosis. | ||||||
SecinH3 | 853625-60-2 | sc-203260 | 5 mg | $278.00 | 6 | |
SecinH3 inhibits VAMP-1 indirectly by interfering with the function of small GTPases involved in vesicle trafficking. By targeting the activity of ADP-ribosylation factors (ARFs), SecinH3 disrupts vesicle transport and exocytosis, indirectly impacting VAMP-1 function. The modulation of intracellular vesicle dynamics by SecinH3 provides insights into potential pathways for regulating neurotransmitter release. | ||||||
Dantrolene | 7261-97-4 | sc-500165 | 25 mg | $350.00 | 7 | |
Dantrolene indirectly inhibits VAMP-1 by targeting intracellular calcium release. As a ryanodine receptor antagonist, Dantrolene reduces calcium levels in the cytoplasm, affecting the SNARE-dependent fusion of synaptic vesicles. By modulating calcium dynamics, Dantrolene indirectly interferes with VAMP-1 function in neurotransmitter release, providing a pharmacological approach to regulate vesicle exocytosis. | ||||||
Dynamin Inhibitor I, Dynasore | 304448-55-3 | sc-202592 | 10 mg | $89.00 | 44 | |
Dynasore inhibits VAMP-1 indirectly by interfering with dynamin, a protein involved in vesicle endocytosis. By targeting dynamin GTPase activity, Dynasore disrupts endocytic processes, indirectly influencing VAMP-1 function in synaptic vesicle recycling. The inhibition of dynamin by Dynasore provides a unique approach to modulating neurotransmitter release by impacting both exocytosis and endocytosis. | ||||||
n-Butylidenephthalide, (E)+(Z) | 551-08-6 | sc-279727 | 10 g | $89.00 | 1 | |
N-Butylidenephthalide inhibits VAMP-1 by disrupting SNARE complex assembly. This natural compound, found in Angelica sinensis, interferes with the interaction between VAMP-1 and other SNARE proteins, leading to the inhibition of vesicle fusion. The specific mechanism of action of N-Butylidenephthalide provides insights into potential natural products that can modulate VAMP-1 function and synaptic vesicle exocytosis. | ||||||
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 inhibits VAMP-1 indirectly by disrupting microtubule dynamics. By interfering with the polymerization of microtubules, Nocodazole impacts vesicle trafficking and SNARE-dependent exocytosis. The modulation of intracellular transport by Nocodazole indirectly influences VAMP-1 function, providing a pharmacological approach to regulate synaptic vesicle exocytosis. | ||||||