Antimicrobial peptides from plants: stabilization of the γ core of a tomato defensin by intramolecular disulfide bond

• Published in: Journal of peptide science 2013-04, Vol.19 (4), p.240-245
• Main Authors: Avitabile, C., Capparelli, R., Rigano, M. M., Fulgione, A., Barone, A., Pedone, C., Romanelli, A.
• Format: Article
• Language: English
• Subjects: Anti-Infective Agents - chemistry; Anti-Infective Agents - pharmacology; antimicrobial; cyclization; Defensins - chemistry; Defensins - pharmacology; Disulfides - chemistry; Helicobacter pylori - growth & development; Lycopersicon esculentum - chemistry; Plant Proteins - chemistry; Plant Proteins - pharmacology; Protein Structure, Secondary; Salmonella enterica - growth & development; tomato defensin
• ISSN: 1075-2617; 1099-1387
• DOI: 10.1002/psc.2479

Cysteine‐containing antimicrobial peptides of diverse phylogeny share a common structural signature, the γ core, characterized by a strong polarization of charges in two antiparallel β sheets. In this work, we analyzed peptides derived from the tomato defensin SolyC07g007760 corresponding to the protein γ 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 Salmonella enterica and Helicobacter pylori. 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 & Sons, Ltd. Oxidation of a plant defensin fragment results in a boomerang‐like structure, in which positive charges necessary for the interaction with the negatively charged lipopolysaccharide (LPS) are exposed.