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Short native antimicrobial peptides and engineered ultrashort lipopeptides: similarities and differences in cell specificities and modes of action

  • Maria Luisa Mangoni
  • Yechiel Shai
Multi-author review

Abstract

Due to the rapid emergence of resistant microbes to the currently available antibiotics, cationic antimicrobial peptides have attracted considerable interest as a possible new generation of anti-infective compounds. However, low cost development for therapeutic or industrial purposes requires, among other properties, that the peptides will be small and with simple structure. Therefore, considerable research has been devoted to optimizing peptide length combined with a simple design. This review focuses on the similarities and differences in the mode of action and target cell specificity of two families of small peptides: the naturally occurring temporins from the skin of amphibia and the engineered ultrashort lipopeptides. We will also discuss the finding that acylation of cationic peptides results in molecules with a more potent spectrum of activity and a higher resistance to proteolytic degradation. Conjugation of fatty acids to linear native peptide sequences is a powerful strategy to engineer novel successful anti-infective drugs.

Keywords

Antimicrobial peptides Lipopeptides LPS-neutralizing activity Mode of action Peptide-membrane interaction Cell-selectivity 

Abbreviations

AMP

Antimicrobial peptide

GFP

Green fluorescent protein

LiPs

Lipopeptides

LPS

Lipopolysaccharide

LPG

Lipophosphoglycan

LTA

Lipoteichoic acid

IM

Inner membrane

MIC

Minimum inhibitory concentration

OM

Outer membrane

TNFα

Tumor necrosis factor alpha

USLiPs

Ultrashort lipopeptides

Notes

Acknowledgments

This study was supported by grants from La Sapienza University of Rome and the Italian Ministero dell’Istruzione, Università e Ricerca (PRIN 2008) and partially by the German Israel Foudation to Y.S. We thank Christopher Angusch for his comments and editing the manuscript.

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Copyright information

© Springer Basel AG 2011

Authors and Affiliations

  1. 1.Istituto Pasteur-Fondazione Cenci BolognettiLa Sapienza University of RomeRomeItaly
  2. 2.Department of Biological ChemistryThe Weizmann Institute of ScienceRehovotIsrael
  3. 3.Dipartimento di Scienze Biochimiche “A. Rossi Fanelli”Università La SapienzaRomeItaly

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