Mambalgin 1

Product Name: Mambalgin 1

CAS No: 1609937-15-6

Purity: 95%

Molar Mass: 6554.5

Chemical Formula: C272H429N85O84S10

Storage: Store at -20 degree Celsius

Sequence: LKCYQHGKVVTCHRDMKFCYHNTGMPFRNLKLILQGCSSSCSETENNKCCSTDRCNK

Application: Mambalgin 1 is a peptide derived from the venom of the black mamba snake (Dendroaspis polylepis), known for its potent analgesic properties. It acts as a selective antagonist of acid-sensing ion channels (ASICs), particularly ASIC1a and ASIC2a, which are involved in pain perception. By blocking these channels, Mambalgin 1 effectively inhibits pain signaling pathways without causing the side effects associated with opioid analgesics. This peptide shows significant promise in the treatment of chronic pain and inflammatory pain conditions. Its unique mechanism of action positions it as a valuable tool in pain research and the development of novel, non-opioid pain therapeutics.

Current Research:

Mambalgin-1 is a peptide isolated from the venom of the black mamba (Dendroaspis polylepis). It functions as a potent inhibitor of acid-sensing ion channels (ASICs), which are involved in pain perception and various neurological processes. The unique analgesic properties of Mambalgin-1, coupled with its specificity for ASICs, have made it a significant focus in pain management research. Mechanism of Action Mambalgin-1 binds to ASICs, particularly ASIC1a, inhibiting their activity by stabilizing the closed state of the channel. This inhibition prevents the influx of cations that would otherwise lead to neuronal excitation and pain signaling. Notably, Mambalgin-1 achieves this without interacting with opioid receptors, thereby avoiding common opioid-related side effects such as respiratory depression and addiction. Analgesic Effects Studies have demonstrated that Mambalgin-1 produces significant analgesic effects in rodent models, comparable to those of morphine. Its ability to alleviate pain without the adverse effects associated with opioids positions it as a promising candidate for developing new pain therapeutics. Structural Insights Recent advancements in structural biology have provided detailed insights into the interaction between Mambalgin-1 and human ASIC1a. Cryo-electron microscopy studies have revealed that Mambalgin-1 binds to the extracellular domain of ASIC1a, inducing conformational changes that lock the channel in a closed state, thereby inhibiting its function. These findings enhance our understanding of the peptide's inhibitory mechanism and facilitate the design of ASIC-targeted analgesics. Potential Therapeutic Applications The specificity of Mambalgin-1 for ASICs, along with its potent analgesic properties, suggests potential therapeutic applications in treating various pain conditions, including inflammatory and neuropathic pain. Additionally, given the role of ASICs in neurological disorders, Mambalgin-1 may have broader applications in neurology. Conclusion Mambalgin-1 represents a novel class of analgesic agents that target ASICs to provide pain relief without the drawbacks of traditional opioids. Ongoing research continues to explore its therapeutic potential and aims to develop Mambalgin-1-based treatments for pain and other neurological conditions.

Reference: Mourier, G., Salinas, M., Kessler, P., Stura, E. A., Leblanc, M., Tepshi, L., ... & Servent, D. (2016). Mambalgin-1 pain-relieving peptide, stepwise solid-phase synthesis, crystal structure, and functional domain for acid-sensing ion channel 1a inhibition. Journal of Biological Chemistry, 291(6), 2616-2629.