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| Description | Lauryl-LF 11 TFA (CAS: 832729-14-3) is the N-terminal lauroyl (C12 fatty acid) synthetic analog of human lactoferrin-derived peptide LF11 (FQWQRNIRKVR), supplied as the TFA salt. Free base C81H134N26O15 (MW 1712.10); TFA salt C83H135F3N26O17 (MW 1826.12). N-terminal lauroylation enhances membrane affinity and LPS binding while retaining the Arg/Trp cationic antibacterial core of LF11. Lauryl-LF 11 shows enhanced anti-Gram-negative activity and endotoxin neutralization with lower hemolysis/cytotoxicity than most cationic peptides. It is a tool for lactoferrin-derived lipopeptide antibiotics and anti-endotoxin drug research. |
| Structure type | N-lauroyl 11-mer (LF11 acylated analog, TFA salt) |
| 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) |
| Lauryl-LF 11 | N-lauroyl LF-11; lauroyl lactoferricin-derived 11-mer; FQWQRNIRKVR-NH2 (N-lauroyl); lipidated lactoferrin AMP | lipidated antimicrobial peptide, lactoferrin-derived, N-acylated, cationic amphipathic peptide, anti-Gram-negative, membrane-targeting, anti-endotoxin, lipopeptide tool | Linear 11-aa cationic lipopeptide, core FQWQRNIRKVR (Phe-Gln-Trp-Gln-Arg-Asn-Ile-Arg-Lys-Val-Arg) derived from human lactoferrin (lactoferricin domain); N-terminus acylated with lauric acid (C12:0), C-terminal Arg amidated; 3 Arg + 1 Lys, net charge +4; one Trp aromatic anchor; no Cys, no disulfide; lauroyl tail confers strong amphipathicity and membrane affinity | C81H134N26O15 | 1711.05 | 1712.13 | TFA (trifluoroacetate); formula and MW calculated for free peptide (with N-lauroyl and C-terminal amide) | 11 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-LLF11-01 | White powder | -20°C, protected from light, desiccated and sealed; Trp is photo-oxidation sensitive - store under Ar/N2 and avoid repeated freeze-thaw; lipopeptide readily absorbs moisture | 2-8°C, protected from light and moisture, stable for several weeks | N-terminal lauroylation greatly increases hydrophobicity, so aqueous solubility is limited. First dissolve in DMSO or DMF to a stock (1-10 mg/mL), then dilute into PBS or water to working concentration; avoid direct aqueous dissolution which causes aggregation. Work in the dark due to Trp photo-oxidation; prepare fresh or aliquot and store at -20°C in the dark; avoid repeated freeze-thaw which causes lipopeptide aggregation/precipitation | solid is relatively stable, but the lauroylated lipopeptide is hygroscopic and Trp is light/oxidation sensitive; long-term storage must be dark, dry, -20°C under inert gas and sealed |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-LLF11-01 | N-lauroylated human lactoferrin peptide LF-11 (FQWQRNIRKVR-NH2), an 11-mer lipopeptide with C-terminal amidation, net charge +4; the acyl tail enhances membrane insertion and bacterial membrane disruption, giving potent bactericidal and anti-endotoxin activity against Gram-negative bacteria including resistant strains. | Lauryl-LF 11 is a lipopeptide obtained by N-terminal lauric acid (C12 fatty acid) acylation and C-terminal amidation of the human lactoferrin-derived 11-mer LF-11 (FQWQRNIRKVR). Its design rationale: native LF-11 is antimicrobial but has limited membrane penetration; introducing a medium-chain acyl tail allows the fatty chain to insert into the bacterial lipid bilayer like a detergent, synergizing with the peptide's cationic charge (3 Arg + 1 Lys, net +4) and Trp aromatic anchoring to markedly destabilize and permeabilize the Gram-negative outer membrane (LPS layer). Studies show the lauroylated derivative has greatly reduced MIC against E. coli, Pseudomonas aeruginosa and other Gram-negatives (including MDR strains), neutralizes LPS, and blocks endotoxin-induced cytokine release. N-acylation also improves protease stability and metabolic half-life. It is a key tool for studying lipo-AMP structure-activity relationships, the balance between acyl chain length and antimicrobial vs hemolytic toxicity, and anti-Gram-negative drug design. | lactoferrin peptide biology, lipopeptide/acylated AMP design, anti-MDR Gram-negative bacteria, anti-endotoxin/sepsis, membrane-targeting mechanism, novel antibiotic lead discovery | bacterial outer membrane LPS, bacterial membrane phospholipids (cardiolipin/phosphatidylethanolamine), endotoxin LPS receptor pathway, bacterial division septum |
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