期刊
FEBS LETTERS
卷 589, 期 19, 页码 2812-2818出版社
WILEY
DOI: 10.1016/j.febslet.2015.08.018
关键词
Antimicrobial peptide; Cationic antimicrobial peptide; Ribosome inactivating protein; Phytolacca dioica
资金
- Second University of Naples (Caserta)
- Italian Cystic Fibrosis Foundation (FFC)
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 PDL4(40-65), 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 PDL4(40-65) is the first antimicrobial peptide identified in a type 1 RIP. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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