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| Description | Polybia-MP1 (CAS: 872043-01-1, MP1) is a 14-residue mastoparan-like peptide isolated from the venom of the Brazilian social wasp Polybia paulista, C-terminally amidated, sequence IDWKKLLDAAKQIL-NH2. Molecular formula C78H132N20O19, MW 1654.03 Da. Unlike typical mastoparans, Polybia-MP1 contains two acidic residues (Asp1, Asp7) with a net charge of only +2 and is non-hemolytic to rat erythrocytes. Polybia-MP1 has moderate mast cell degranulation activity, polymorphonuclear leukocyte chemotactic activity, and antifungal and anti-biofilm activity against Candida albicans and Cryptococcus neoformans. Recent studies show Polybia-MP1 has selective cytotoxicity against melanoma cells through membrane disruption and apoptosis induction, serving as a research model for membrane-active peptide selectivity design. |
| Structure type | Linear 14-mer (C-amidated P. paulista venom mastoparan, net charge +2) |
| Solubility | Readily soluble in water, DMSO |
| Storage | Powder -20C, dry, protected from light |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| Polybia-MP1 (Polybia-Mastoparan I) | MP1; Polybia-MPI; wasp-venom mastoparan | Antimicrobial, antibacterial, antifungal, antitumor, mast cell degranulation, membrane-active, low hemolysis | Linear 14-aa cationic amphipathic α-helical mastoparan-family peptide; C-terminally amidated (–NH₂); net charge +1 (3 Lys − 2 Asp); contains 1 Trp (Trp3) and 3 Leu; folds into amphipathic α-helix in membrane environments; selective for bacterial and tumor cell membranes over normal mammalian erythrocytes (low hemolysis) | C₇₈H₁₃₂N₂₀O₁₉ (amide form) | 1653.00 | 1654.04 | TFA salt (commercial standard) | 14 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-PMP1-01 | White powder | Store at -20°C, sealed, desiccated, protected from light. Aliquot to avoid repeated freeze-thaw. Due to Trp3 (light-sensitive), recommend inert gas (Ar/N2) headspace. | 2–8°C for short-term use; working aliquots at -20°C; stable for shipping at ambient. | Soluble in DMSO and ethanol (≥10 mg/mL), sparingly soluble in neutral PBS (~1–10 mg/mL). Prepare stock in DMSO then dilute into aqueous buffer. Contains 1 Trp (Trp3) prone to photo-oxidation-protect from light; prepare fresh or store aliquots at -20°C. No Cys or Met-no disulfide or oxidation concerns. | Stable as solid at -20°C, desiccated and protected from light. Hygroscopic-keep desiccated. |
Functional Description
| Product Code | Frontend Short Summary (for search list display) | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-PMP1-01 | A 14-aa C-amidated mastoparan-family wasp-venom peptide from Polybia paulista, with broad-spectrum bacteria-selective membrane disruption, low hemolysis, and antitumor activity. | Polybia-MP1 is a cationic amphipathic α-helical peptide isolated from the venom of the social wasp Polybia paulista, belonging to the mastoparan family. It has broad-spectrum activity against both Gram-positive and Gram-negative bacteria. Its most striking feature is high selectivity for bacterial and tumor cell membranes over normal mammalian erythrocytes-attributed to the anionic phospholipid-rich surface (phosphatidylserine PS, phosphatidylethanolamine PE) of bacteria/tumor cells, versus the neutral outer leaflet of normal cell membranes. Polybia-MP1 disrupts membrane integrity via toroidal pore or detergent-like mechanisms. It also has antifungal and antitumor activity and activates G-protein-coupled mast cell degranulation. Due to its high selectivity and low hemolysis, Polybia-MP1 is an important lead for developing novel antimicrobial and anticancer peptide therapeutics. | Antimicrobial peptide design, antibiotic alternatives, oncology/peptide therapeutics, venom biochemistry, membrane biophysics, selective tumor cell targeting | Anionic bacterial/tumor membranes (PS, PE-rich lipids); toroidal pore/detergent-like membrane disruption; G-protein-coupled mast cell degranulation |
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