Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2047438 | FEBS Letters | 2015 | 7 Pages |
Abstract
We investigated the antimicrobial activity of PD-L4, a type 1 RIP from Phytolacca dioica. We found that this protein is active on different bacterial strains both in a native and denatured/alkylated form and that this biological activity is related to a cryptic peptide, named PDL440-65, identified by chemical fragmentation. This peptide showed the same antimicrobial activity of full-length protein and possessed, similarly to several antimicrobial peptides, an immunomodulatory effect on human cells. It assumes an alpha-helical conformation when interact with mimic membrane agents as TFE and likely bacterial membranes are a target of this peptide. To date PDL440-65 is the first antimicrobial peptide identified in a type 1 RIP.
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Authors
Elio Pizzo, Anna Zanfardino, Antonella M.A. Di Giuseppe, Andrea Bosso, Nicola Landi, Sara Ragucci, Mario Varcamonti, Eugenio Notomista, Antimo Di Maro,