Next Article in Journal
Allosteric Modulation of αβδ GABAA Receptors
Next Article in Special Issue
Cell-Penetrating Penta-Peptides (CPP5s): Measurement of Cell Entry and Protein-Transduction Activity
Previous Article in Journal
Multiple Routes to Oestrogen Antagonism
Previous Article in Special Issue
Building Cell Selectivity into CPP-Mediated Strategies
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,*
1 Laboratoire de Chimie Biologique et Médicale et de Microbiologie Pharmaceutique, Institut de Pharmacie, Université Libre de Bruxelles, Boulevard du Triomphe, CP 205/3, B-1050 Brussels, Belgium 2 Laboratoire de Structure et Fonction des Membranes Biologiques, Faculté des Sciences, Université Libre de Bruxelles, Boulevard du Triomphe, CP 206/2, B-1050 Brussels, Belgium 3 Biological Nanosystems, Interdisciplinary Research Institute, University of Sciences and Technology Lille, USR3078 CNRS, 50 Avenue Halley, F-59658 Villeneuve d’Ascq, France
* Author to whom correspondence should be addressed.
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)
View Full-Text   |   Download PDF [948 KB, uploaded 1 November 2010]   |   Browse Figure

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.

Share & Cite This Article

Export to BibTeX |
EndNote


MDPI and ACS Style

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.

View more citation formats

Related Articles

Article Metrics

Comments

Citing Articles

[Return to top]
Pharmaceuticals EISSN 1424-8247 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert