Ultrashort antibacterial and antifungal lipopeptides.

Abstract:

:Host-defense cationic antimicrobial peptides ( approximately 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. (iii) 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.

authors

Makovitzki A,Avrahami D,Shai Y

doi

10.1073/pnas.0606129103

subject

Has Abstract

pub_date

2006-10-24 00:00:00

pages

15997-6002

issue

43

eissn

0027-8424

issn

1091-6490

pii

0606129103

journal_volume

103

pub_type

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