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Updated: Apr 21, 2026

Production and Visualization of Bacterial Spheroplasts and Protoplasts to Characterize Antimicrobial Peptide Localization
Published on: August 11, 2018
Antimicrobial activity of peptides derived from olive flounder lipopolysaccharide binding protein/bactericidal
Bo-Hye Nam1, Ji-Young Moon2, Eun-Hee Park3
1Biotechnology Research Division, National Fisheries Research and Development Institute, Haean-ro 216, Gijang-eup, Gijang-gun, Busan 619-705, Korea. nambohye@korea.kr.
Abstract:
We describe the antimicrobial function of peptides derived from the C-terminus of the olive flounder LBP BPI precursor protein. The investigated peptides, namely, ofLBP1N, ofLBP2A, ofLBP4N, ofLBP5A, and ofLBP6A, formed α-helical structures, showing significant antimicrobial activity against several Gram-negative bacteria, Gram-positive bacteria, and the yeast Candida albicans, but very limited hemolytic activities. The biological activities of these five analogs were evaluated against biomembranes or artificial membranes for the development of candidate therapeutic agents. Gel retardation studies revealed that peptides bound to DNA and inhibited migration on an agarose gel. In addition, we demonstrated that ofLBP6A inhibited polymerase chain reaction. These results suggested that the ofLBP-derived peptide bactericidal mechanism may be related to the interaction with intracellular components such as DNA or polymerase.
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