LL-37

Purity: >98% (HPLC on request) | Molecular Formula: C205H340N60053
Molecular Weight: 4493.33 g/mol | Sequence: Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys- Glu-Phe-Lys-Arg-Ile-Val-GIn-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser

Content & Potency: 2000mcg/ml subcutaneous injection provided in a 5ml vial.

Membrane Core-Specific Antimicrobial Action of Cathelicidin LL-37 Peptide Switches Between Pore and Nanofibre Formation Membrane-disrupting antimicrobial peptides provide the membrane forming lipids. We demonstrate that LL-37 broad-spectrum defence against localized bacterial invasion exhibits two distinct interaction pathways: pore formation in a range of hosts including humans. The most generally in bilayers of unsaturated phospholipids and membrane held consensus is that targeting to pathogens is based on modulation with saturated phospholipids. Uniquely, the interactions with the head groups of membrane lipids. Here membrane modulation yields helicalrich fibrous we show that the action of LL-37, a human peptide-lipid superstructures. Our results point at antimicrobial peptide switches the mode of action based on alternative design strategies for peptide antimicrobials. the structure of the alkyl chains, and not the head groups of Shahmiri, Mahdi & Enciso, Marta & Adda, Christopher & Smith, Brian & Perugini, Matthew & Mechler, Adam. (2016). Membrane Core-Specific Antimicrobial Action of Cathelicidin Lt-/ leptide Switches between l’ore and Nanohbre Formation. Scientine Keports.