Mastoparan peptide – Potent antimicrobial peptide
Mastoparan peptide is a 14-residue cationic peptide toxin isolated from the wasp Vespula lewisii venom which shows an important potency as an antimicrobial and anticancer agent but also as a Cell Permeable Peptide.
Mastoparan is mainly known to be a receptor-independant and allosteric regulator of G-protein by stimulating GTPase activity.
Besides modulating the activity of G-protein, Mastoparan have the ability to bind other intracellular targets such as Ca2+-ATP (implicated in Ca2+ release), small GTP binding proteins rho and rac, and many others.
Mastoparan also belongs to the cell permeable peptide (CPP) family. As such, Mastoparan increases the membrane conductance and permeability of planar lipid bilayer and liposomal membranes which leads to enhanced the penetration of Ca2+, Na+ or K+ ions.
Mastoparan peptide have also a potential antibiotic effect due to its potent antimicrobial activity which can turn Mastoparan peptide to a potential drug for infectious diseases.
Some studies have also reported that Mastoparan peptide exhibits potent anti-cancer activities toward leukemia, myeloma, and breast cancer cells with an approximately half maximal inhibitory concentration (IC50) of 9µM, 11µM and 22µM respectively.
Mastoparan peptide have shown to be more specific to cancer cells than to normal cells.
Sequence : INLKALAALAKKIL-NH2|
MW : 1 478.9 Da (C70H131N19O15)|
Purity : > 95%|
Counter-Ion : TFA Salts (see option TFA removal)|
Delivery format : Freeze dried in propylene 2mL microtubes|
Other names : NSC351907, 72093-21-1, CHEMBL1964493, NSC-351907, NCGC00163465-01|
Peptide Solubility Guideline|
Bulk peptide quantities available|
Price € HT|
Price $ USD|
1- Yamamoto T, Ito M, Kageyama K, et al. FEBS J. (2014)
Mastoparan Peptide Causes Mitochondrial Permeability Transition Not by Interacting With Specific Membrane Proteins but by Interacting With the Phospholipid Phase
BACKGROUND: The mastoparan peptide is known as an inducer of the mitochondrial permeability transition. Although mastoparan was suggested to interact with a proteinaceous target in mitochondria to induce this transition, the action sites of mastoparan have not yet been investigated.
OBJECTIVE: Clarify whether specific interactions of mastoparan with receptors or enzymes are associated with the induction of this permeability transition,
METHOD/RESULTS: We examined the effects of d-isomeric peptides, which were synthesized using d-amino acids assembled in endogenous (inverso mastoparan) and reverse (retro-inverso mastoparan) orientations. When we added inverso mastoparan to isolated mitochondria, the peptide caused the permeability transition in a partially cyclosporin A-sensitive manner at lower doses and in a cyclosporin A-insensitive manner at higher ones. The manners of action and the potencies of inverso mastoparan were close to those of parent mastoparan, indicating that the targets of mastoparan for induction of the permeability transition were neither receptors, nor enzymes in the mitochondria. Retro-inverso mastoparan also had the same effect on the mitochondria as mastoparan, although the potencies of the effect were weaker. Not only on mitochondria, but also on phospholipid vesicles, mastoparan and inverso mastoparan showed massive permeabilization effects at the same potencies, although retro-inverso mastoparan showed weaker ones.
CONCLUSION: These results indicate that mastoparan interacted with the phospholipid phase of the mitochondrial membrane (and not with specific proteins) to induce the permeabilization in cyclosporin A-sensitive and -insensitive manners.
2- Tohkin M, Yagami T, Matsubara T. FEBS Lett. (1990)
Mastoparan, a Peptide Toxin From Wasp Venom, Stimulates Glycogenolysis Mediated by an Increase of the Cytosolic Free Ca2+ Concentration but Not by an Increase of cAMP in Rat Hepatocytes
BACKGROUND: A wasp venom, mastoparan, rapidly increased the cytosolic free Ca2+ concentration [( Ca2+]i) and activated phosphorylase in rat hepatocytes in a concentration-dependent manner. Mastoparan could increase [Ca2+]i even in the absence of extracellular Ca2+, but a larger increase was observed in the presence of extracellular Ca2+. Thus, mastoparan mobilized Ca2+ from intracellular and extracellular Ca2+ stores. It also activated inositol triphosphate (IP3) accumulation, but did not stimulate cAMP production.
CONCLUSION: From these results, we conclude that mastoparan activates rat hepatic glycogenolysis mediated by the accumulation of IP3, which causes an increase of [Ca2+]i but not that mediated by cAMP.