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| Description | LS-BF1 (CAS: 2892148-58-0) is a stable, low-toxicity cationic antimicrobial peptide engineered from cathelicidin-BF of the banded krait (Bungarus fasciatus) venom, molecular formula C107H166N28O15, MW 2084.64 Da. Native cathelicidin-BF is a 30-residue Lys/Phe-rich peptide (KFFRKLKKSVKKRAKEFFKKPRVIGVSIPF) and a potent snake venom peptide antibiotic. Through truncation and stabilization engineering, LS-BF1 retains broad-spectrum antibacterial activity while markedly reducing hemolysis and cytotoxicity and improving protease stability. LS-BF1 is active against multidrug-resistant Gram-negative and Gram-positive bacteria, serving as a tool for studying snake venom cathelicidin optimization and anti-resistant-pathogen peptide drug development. |
| Structure type | Engineered linear cationic peptide (stabilized truncated analog of cathelicidin-BF) |
| Solubility | Readily soluble in water, dilute acetic acid |
| 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) |
| LS-BF1 | LSBF1; VKRFKKFFRKFKKFV-NH2 | Antimicrobial peptide, Cationic peptide, α-helical, Stapled peptide, Membrane-lytic, Low toxicity, In vivo efficacy, Anti-drug-resistant bacteria | Stapled peptide, linear sequence VKRFKKFFRKFKKFV (15 aa), C-terminal amidated (-NH2); net charge +8 (6 Lys + 2 Arg, no acidic residues); Lys6 and Lys10 side chains cross-linked via an (E)-but-2-enyl bridge to stabilize α-helical conformation; Phe-rich (5 Phe) with 2 Val, hydrophobic residues account for 47%; amphipathic α-helix where high cationic charge and strong hydrophobic face act synergistically on bacterial membranes | C107H166N28O15 | 2083.31 | 2084.69 | TFA salt (trifluoroacetate) | 15 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-PP113-09 | White powder | -20°C, protected from light, dry, sealed | 2-8°C, protected from light, stable for 1-2 weeks | Soluble in sterile water or dilute acetic acid (0.1% AcOH); high cationic charge (+8) provides good aqueous solubility, but high hydrophobic residue content (47%) may cause partial precipitation in PBS - prepare stock in sterile water or dilute AcOH, dilute with buffer before use; no Cys/Met/Trp/Tyr residues, low oxidation and photo-oxidation risk; hydrocarbon staple bridge stable in aqueous solution and unaffected by reducing agents; C-terminal amidation enhances stability; aliquot and store at -80°C, avoid repeated freeze-thaw | Solid powder stable for 3 years at -20°C under dry, dark conditions; hydrocarbon staple bridge highly chemically stable; no oxidizable residues, stable in solid state; seal and protect from moisture |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-PP113-09 | LS-BF1, a 15-residue hydrocarbon-stapled α-helical cationic antimicrobial peptide with C-terminal amidation, potent activity against drug-resistant bacteria, low toxicity, and in vivo efficacy | LS-BF1 is an engineered hydrocarbon-stapled antimicrobial peptide in which an (E)-but-2-enyl bridge between Lys6 and Lys10 side chains locks the α-helical conformation. This staple significantly enhances proteolytic stability and membrane penetration capability. LS-BF1 is a highly cationic peptide (net charge +8) that kills bacteria rapidly through a membrane-disruption mechanism: it first binds to negatively charged bacterial membrane lipids (phosphatidylglycerol, LPS), then inserts into the lipid bilayer causing membrane permeabilization and content leakage. The peptide exhibits potent antibacterial activity against multiple multidrug-resistant Gram-positive and Gram-negative strains. Key advantages include: (1) low eukaryotic cytotoxicity and hemolytic activity; (2) resistance to proteolytic degradation conferred by the hydrocarbon staple; (3) good in vivo antibacterial efficacy in mouse infection models. LS-BF1 represents a strategy of engineering natural AMPs via stapling chemistry to overcome pharmacokinetic limitations, and is an important candidate for next-generation anti-drug-resistant therapeutics. | Antimicrobial peptide development, Anti-drug-resistant bacteria, Stapled peptide drug design, α-helical peptide, Anti-infective therapy, In vivo efficacy evaluation, Membrane-active peptide | Bacterial cell membrane (phosphatidylglycerol, LPS); Membrane lysis/permeabilization; Hydrocarbon staple stabilizes α-helix |
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