Premium
Two antimicrobial and nematicidal peptides derived from sequences encoded Picea sitchensis
Author(s) -
Liu Rui,
Mu Lixian,
Liu Huan,
Wei Lin,
Yan Tianhua,
Chen Ming,
Zhang Keyun,
Li Jianxu,
You Dewen,
Lai Ren
Publication year - 2011
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1380
Subject(s) - antimicrobial , candida albicans , bacillus subtilis , antimicrobial peptides , biochemistry , escherichia coli , hemolysis , amino acid , microbiology and biotechnology , chemistry , staphylococcus aureus , peptide , biology , bacteria , genetics , gene , immunology
Two antimicrobial peptides (piceain 1 and 2) derived from sequences encoded Picea sitchensis are identified. Their amino acid sequences are KSLRPRCWIKIKFRCKSLKF and RPRCWIKIKFRCKSLKF, respectively. One intra‐molecular disulfide bridge is formed by these two half‐cysteines in both piceain 1 and 2. Antimicrobial activities of synthesized piceains against several kinds of microorganisms were tested. They showed antimicrobial activities against Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus , and fungus Candida albicans but little antimicrobial activity against Bacillus subtilis . The results of nematicidal test showed they exerted strong nematicidal activities against Caenorhabditis elegans , following exposure for 5 h at concentrations as low as 10 µg/ml. They had weak hemolytic abilities against human and rabbit red cells. At the concentration of 250 µg/ml, they induced red cell hemolysis of less than 5%. Circular dichroism spectra of the two antimicrobial peptides were investigated in several solutions. Their main secondary structure components are β‐sheet and random. The current work provides a novel family of antimicrobial and nematicidal peptides with unique disulfided loop containing nine amino acid residues. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.