Short native antimicrobial peptides and engineered ultrashort lipopeptides: similarities and differences in cell specificities and modes of action |
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Authors: | Maria Luisa Mangoni Yechiel Shai |
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Institution: | 1.Istituto Pasteur-Fondazione Cenci Bolognetti,La Sapienza University of Rome,Rome,Italy;2.Department of Biological Chemistry,The Weizmann Institute of Science,Rehovot,Israel;3.Dipartimento di Scienze Biochimiche “A. Rossi Fanelli”,Università La Sapienza,Rome,Italy |
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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. |
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Keywords: | |
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