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| Description | CaLL is a novel hybrid antimicrobial peptide designed based on cecropin A, LL-37, and magainin II, with CAS number 1228093-67-1, sequence Lys-Trp-Lys-Leu-Phe-Lys-Lys-Ile-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg (one-letter: KWKLFKKIFKRIVQRIKDFLR), totaling 21 amino acid residues, with a theoretical molecular weight of 2791.47 Da and molecular formula C₁₃₆H₂₂₄N₃₈O₂₅. CaLL is a representative product of antimicrobial peptide engineering (hybrid peptide design), combining structural features of three classic antimicrobial peptides: the N-terminal sequence features of cecropin A, the cationic amphipathic features of LL-37, and the membrane-active features of magainin II. The sequence contains 5 lysine residues and 4 arginine residues, with abundant cationic residues and strong positive charge. CaLL exhibits antibacterial activity against Bacillus anthracis (including its vegetative form) and Burkholderia cepacia, with minimum inhibitory concentrations (MIC) of 7.8, 31.3, and 31.3 μg/mL, respectively. The antimicrobial mechanism of CaLL primarily involves disruption of bacterial cell membranes: as a cationic antimicrobial peptide, CaLL interacts electrostatically with negatively charged components on the bacterial cell membrane surface through its positively charged lysine and arginine residues, then inserts into the lipid bilayer through the hydrophobic face, leading to increased membrane permeability and content leakage, ultimately resulting in bacterial death. CaLL is widely used in hybrid antimicrobial peptide design research, antimicrobial peptide structure-activity relationship research, Bacillus infection prevention research, and novel antibacterial drug development. |
| Molecular formula | C₁₃₆H₂₂₄N₃₈O₂₅ |
| Molecular weight (Da) | 2791.47 |
| Structure type | Linear 21-mer peptide (hybrid antimicrobial peptide based on cecropin A/LL-37/magainin II, containing 5 lysines and 4 arginines, strongly cationic, anti-Bacillus anthracis) |
| Solubility | Freely soluble in water, PBS, DMSO |
| Storage | -20°C, 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) |
| Melittin free acid | Melittin free acid; major active peptide of bee venom | Bee venom peptide, membrane-active peptide, hemolytic peptide, antimicrobial peptide, anticancer peptide | Classical amphipathic α-helical 26-mer peptide derived from honeybee venom, with a free C-terminal carboxyl (non-natural amidation modification); potently lyses cell membranes via the carpet model with strong hemolytic activity, and also has broad-spectrum antibacterial, anticancer, anti-inflammatory and immune adjuvant activities, serving as a classic model molecule for membrane peptide research | C₁₃₁H₂₂₉N₃₉O₃₁ | 2846.75 | ~2848.6 | Free peptide | 26 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-MELFA | White powder | Store at -20°C, sealed, dry and protected from light. Aliquot for storage. | Stable for 1 month at 2–8°C in sealed dry condition; stable for shipping at ambient temperature. | Stable for 7 days at 4°C. Soluble in dilute acetic acid, acidic buffers and water. Highly membrane-active; induces hemolysis at low concentrations. Avoid co-incubation with erythrocytes and eukaryotic cells. Maximal hemolytic activity under acidic conditions. | Stable for 2 years at -20°C, dry and protected from light. |
Functional Description
| Product Code | Frontend Short Summary (for search list display) | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-MELFA | Melittin free acid with potent membrane lysis, antibacterial and anticancer activity | Melittin free acid is a free-carboxyl variant of melittin, a classical amphipathic α-helical membrane-active peptide. It potently lyses cell membranes via the carpet model with pronounced hemolytic activity, and has rapid bactericidal activity against both Gram-positive and Gram-negative bacteria. It also inhibits tumor proliferation, induces apoptosis and acts as an immune adjuvant. | Membrane biophysics, bee venom pharmacology, anticancer peptides, antimicrobial peptides, immune adjuvants | Carpet model membrane lysis; tumor cell apoptosis pathway; hemolysis and membrane perforation |
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