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

Pharmaceuticals

Michèle Seil¹  Carole Nagant¹  Jean-Paul Dehaye¹  Michel Vandenbranden² 

[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;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

关键词: antimicrobial peptides;    biofilm;    P2X₇ receptors;    formyl peptide receptors;    cell-penetrating peptides;    LL-37;    cathelicidin;   

DOI  :  10.3390/ph3113435

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2010 by the authors; licensee MDPI, Basel, Switzerland.