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Antinematodal effect of antimicrobial peptide, PMAP‐23, isolated from porcine myeloid against Caenorhabditis elegans
Author(s) -
Park Yoonkyung,
Jang SeungHwan,
Lee Dong Gun,
Hahm KyungSoo
Publication year - 2004
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.518
Subject(s) - antimicrobial , peptide , myeloid , chemistry , myeloid cells , antimicrobial peptides , microbiology and biotechnology , biology , biochemistry , cancer research
Abstract The antinematodal activity and mechanism of a 23‐mer antimicrobial peptide, PMAP‐23, derived from pig myeloid was investigated. PMAP‐23 displayed a strong antinematodal activity against the eggs and worms of Caenorhabditis elegans . To investigate the antinematodal mechanism of PMAP‐23, fluorescence activated flow cytometry and confocal laser scanning microscopy were performed. C. elegans treated with PMAP‐23 showed higher fluorescence intensity by propidium iodide (PI) staining than normal cells. Confocal microscopy showed that the peptide was localized in the egg's shell and cell membrane. The action of the peptide against C. elegans membranes was examined by testing the membrane disrupting activity using liposome (PC/PS; 3:1, w/w). The result suggests that PMAP‐23 may exert its antinematodal activity by disrupting the structure of the cell membrane via pore formation or via direct interaction with the lipid bilayers. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.