Ultrashort antibacterial and antifungal lipopeptides

Arik Makovitzki, Dorit Avrahami, Yechiel Shai

Research output: Contribution to journalArticlepeer-review

416 Scopus citations


Host-defense cationic antimicrobial peptides (≈12-50 aa long) play an essential protective role in the innate immune system of all organisms. Lipopeptides, however, are produced only in bacteria and fungi during cultivation, and they are composed of specific lipophilic moieties attached to anionic peptides (six to seven amino acids). Here we report the following. (i) The attachment of an aliphatic chain to otherwise inert, cationic D,L tetrapeptides endows them with potent activity against various microorganisms including antibiotic resistance strains. (ii) Cell specificity is determined by the sequence of the short peptidic chain and the length of the aliphatic moiety. (ii) Despite the fact that the peptidic chains are very short, their mode of action involves permeation and disintegration of membranes, similar to that of many long antimicrobial peptides. Besides adding important information on the parameters necessary for host-defense lipopeptides to kill microorganisms, the simple composition of these lipopeptides and their diverse specificities should make them economically available, innate immunity-mimicking antimicrobial and antifungal compounds for various applications.

Original languageEnglish
Pages (from-to)15997-16002
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number43
StatePublished - 24 Oct 2006
Externally publishedYes


  • Antimicrobial peptides
  • Carpet model
  • Innate immunity
  • Lytic peptides
  • Peptide-membrane interaction


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