Mastoparan-V is a wasp-venom-derived amphipathic peptide with strong helix-forming propensity. The sequence enhances membrane interaction through hydrophobic and cationic balance. Researchers study its lytic activity, conformational changes, and peptide-lipid dynamics. Applications include membrane-active peptide research, toxin-motif analysis, and helix-bilayer modeling.
CAT No: R2387
CAS No:72093-22-2
Synonyms/Alias:Mastoparan X;72093-22-2;mastoparan-V;MP-V;CHEBI:78519;AKOS024456837;PD079195;mast cell degranulating peptide (Vespa velutina);Q27147845;Ile-Asn-Trp-Lys-Gly-Ile-Ala-Ala-Met-Ala-Lys-Lys-Leu-Leu-NH2;L-isoleucyl-L-asparaginyl-L-tryptophyl-L-lysylglycyl-L-isoleucyl-L-alanyl-L-alanyl-L-methionyl-L-alanyl-L-lysyl-L-lysyl-L-leucyl-L-leucinamide;
Mastoparan-V is a biologically active peptide originally isolated from the venom of the wasp species Vespa magnifica. As a member of the mastoparan family, it is characterized by its amphipathic helical structure and its ability to interact with cellular membranes, making it a valuable tool in the study of membrane dynamics and signal transduction. Researchers are particularly interested in mastoparan-V due to its potent modulatory effects on G-protein coupled receptor (GPCR) pathways and its role in promoting cellular responses such as degranulation, secretion, and membrane permeability. Its distinctive sequence and physicochemical properties provide a versatile platform for investigating peptide-membrane interactions, intracellular signaling mechanisms, and the development of novel biomimetic molecules.
Membrane Permeabilization Studies: Mastoparan-V is frequently employed as a model peptide for elucidating the mechanisms underlying membrane disruption and permeabilization. Due to its amphipathic structure and cationic nature, it can insert into lipid bilayers and induce pore formation. This property is instrumental for researchers investigating the biophysical principles of membrane integrity, peptide-lipid interactions, and the design of synthetic peptides with tailored membrane activity for drug delivery or antimicrobial research.
G-Protein Activation Research: The peptide is a well-established probe for the direct activation of heterotrimeric G-proteins independent of receptor engagement. By mimicking receptor-mediated activation, mastoparan-V enables the dissection of downstream signaling cascades in cellular systems. Its use facilitates the characterization of G-protein function, mapping of effector pathways, and screening of modulators that influence G-protein signaling, which are critical areas in cell biology, pharmacology, and signal transduction research.
Cellular Secretion and Exocytosis Assays: Mastoparan-V is widely utilized to stimulate exocytosis and secretion in various cell types, including mast cells and neuroendocrine cells. Through its action on membrane and signaling proteins, it triggers the release of intracellular granule contents, providing a robust experimental model for studying the molecular mechanisms of vesicular trafficking, fusion, and regulated secretion. These assays are essential for understanding fundamental processes in immunology, endocrinology, and neurobiology.
Peptide Structure-Activity Relationship (SAR) Analysis: The unique sequence motifs and functional domains of mastoparan-V make it a valuable template for structure-activity relationship studies. Researchers use it to design and evaluate peptide analogs with altered biological activities, aiming to improve selectivity, potency, or stability. SAR investigations contribute to the rational development of new peptide-based research tools and the exploration of structure-function relationships in bioactive peptides.
Synthetic Peptide Development: Mastoparan-V serves as a benchmark in the synthesis and characterization of amphipathic peptides. Its well-defined secondary structure and membrane-active properties guide the optimization of synthetic protocols and purification strategies in peptide chemistry. By using it as a reference, peptide chemists can evaluate novel synthetic methodologies, assess conformational stability, and advance the engineering of functional peptides for a broad range of biochemical applications.
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