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Pharmaceuticals 2010, 3(11), 3435-3460; doi:10.3390/ph3113435
Review

Spotlight on Human LL-37, an Immunomodulatory Peptide with Promising Cell-Penetrating Properties

1, 1, 1, 2 and 3,*
Received: 4 October 2010 / Revised: 23 October 2010 / Accepted: 29 October 2010 / Published: 1 November 2010
(This article belongs to the Special Issue Cell-penetrating Peptides)
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Abstract

Cationic antimicrobial peptides are major components of innate immunity and help control the initial steps of the infectious process. They are expressed not only by immunocytes, but also by epithelial cells. They share an amphipathic secondary structure with a polar cationic site, which explains their tropism for prokaryote membranes and their hydrophobic site contributing to the destructuration of these membranes. LL-37 is the only cationic antimicrobial peptide derived from human cathelicidin. LL-37 can also cross the plasma membrane of eukaryotic cells, probably through special domains of this membrane called lipid rafts. This transfer could be beneficial in the context of vaccination: the activation of intracellular toll-like receptors by a complex formed between CpG oligonucleotides and LL-37 could conceivably play a major role in the building of a cellular immunity involving NK cells.
Keywords: antimicrobial peptides; biofilm; P2X7 receptors; formyl peptide receptors;
cell-penetrating peptides; LL-37; cathelicidin
antimicrobial peptides; biofilm; P2X7 receptors; formyl peptide receptors;
cell-penetrating peptides
; LL-37; cathelicidin
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Seil, M.; Nagant, C.; Dehaye, J.-P.; Vandenbranden, M.; Lensink, M.F. Spotlight on Human LL-37, an Immunomodulatory Peptide with Promising Cell-Penetrating Properties. Pharmaceuticals 2010, 3, 3435-3460.

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