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

Cellular and Molecular Life Sciences - Tập 68 - Trang 2267-2280 - 2011
Maria Luisa Mangoni1,2, Yechiel Shai3
1Istituto Pasteur-Fondazione Cenci Bolognetti, La Sapienza University of Rome, Rome, Italy
2Dipartimento di Scienze Biochimiche “A. Rossi Fanelli”, Università “La Sapienza”, Rome, Italy
3Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel

Tóm tắt

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.

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