Antimicrobial peptides from plants: stabilization of the γ core of a tomato defensin by intramolecular disulfide bond‡. (19th February 2013)

• Record Type: Journal Article
• Authors: Avitabile, C.; Capparelli, R.; Rigano, M. M.; Fulgione, A.; Barone, A.; Pedone, C.; Romanelli, A.; Morelli, Giancarlo
• Is Part Of: Journal of peptide science. Volume 19:Number 4(2013:Apr.)
• Page Start: 240
• Page End: 245
• Publication Date: 2013-02-19
• Subjects: Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.2479
• Languages: English
• ISSNs: 1075-2617

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Cysteine‐containing antimicrobial peptides of diverse phylogeny share a common structural signature, the <italic>γ</italic> core, characterized by a strong polarization of charges in two antiparallel <italic>β</italic> sheets. In this work, we analyzed peptides derived from the tomato defensin SolyC07g007760 corresponding to the protein <italic>γ</italic> core and demonstrated that cyclization of the peptides, which results in segregation of positive charges to the turn region, produces peptides very active against Gram negative bacteria, such as <italic>Salmonella enterica</italic> and <italic>Helicobacter pylori</italic>. Interestingly, these peptides show very low hemolytic activity and thus represent a scaffold for the design of new antimicrobial peptides. Copyright © 2013 European Peptide Society and John Wiley &amp; Sons, Ltd.</p> </abstract>