LL-37 Is an anti-microbial peptide which belongs to the cathelicidin family of
AMPs(anti-microbial peptides). LL-37, like cathelicidins, are stored in neutrophil
granules as inactive precursors and are released as mature peptides when
neutrophils are stimulated. LL-37 is expressed in various cells and tissues such as
circulating neutrophils and myeloid bone marrow cells, epithelial cells of the skin, and
is also expressed in the gastrointestinal tract, as well as in the epididymis and lungs.
Moreover, production of LL-37 in macrophages is stimulated by vitamin D released
by sunlight through the skin. LL-37 plays an important role in the first line of defense
against infection and systemic invasion of pathogens at sites of inflammation and
wound. It is cytotoxic to both bacterial and normal eukaryotic cells and is significantly
resistant to proteolytic degradation in solution. LL-37 shows a broad spectrum of
antimicrobial activity against bacteria, enveloped viruses, and fungi. It has also
demonstrated success in helping promote wound healing and it may play a negative
role in atopic dermatitis and apsoriasis.


Content & Potency: 200mg capsules provided in quantities of 90
Suggested dosage: Varies with indication and patient


Membrane Core-Specific Antimicrobial Action of Cathelicidin LL-37 Peptide
Switches Between Pore and Nanofibre Formation


Membrane-disrupting antimicrobial peptides provide broad-spectrum defence
against localized bacterial invasion in a range of hosts including humans. The most
generally held consensus is that targeting to pathogens is based on interactions
with the head groups of membrane lipids. Here we show that the action of LL-37, a
human antimicrobial peptide switches the mode of action based on the structure of
the alkyl chains, and not the head groups of the membrane forming lipids. We
demonstrate that LL-37 exhibits two distinct interaction pathways: pore formation in
bilayers of unsaturated phospholipids and membrane modulation with saturated
phospholipids. Uniquely, the membrane modulation yields helical-rich fibrous
peptide-lipid superstructures. Our results point at alternative design strategies for
peptide antimicrobials.

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