title: Antimicrobial activity of peptides derived from olive flounder lipopolysaccharide binding protein/bactericidal permeability-increasing protein (LBP/BPI).
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.
authors.affiliation: Biotechnology Research Division, National Fisheries Research and Development Institute, Haean-ro 216, Gijang-eup, Gijang-gun, Busan 619-705, Korea. nambohye@korea.kr.
authors.forename: Bo-Hye
authors.initials: BH
authors.lastname: Nam
authors.affiliation: Biotechnology Research Division, National Fisheries Research and Development Institute, Haean-ro 216, Gijang-eup, Gijang-gun, Busan 619-705, Korea. moonjy@nfrdi.go.kr.
authors.forename: Ji-Young
authors.initials: JY
authors.lastname: Moon
authors.affiliation: Biotechnology Research Division, National Fisheries Research and Development Institute, Haean-ro 216, Gijang-eup, Gijang-gun, Busan 619-705, Korea. 549@nfrdi.go.kr.
authors.forename: Eun-Hee
authors.initials: EH
authors.lastname: Park
authors.affiliation: Biotechnology Research Division, National Fisheries Research and Development Institute, Haean-ro 216, Gijang-eup, Gijang-gun, Busan 619-705, Korea. yokim@nfrdi.go.kr.
authors.forename: Young-Ok
authors.initials: YO
authors.lastname: Kim
authors.affiliation: Biotechnology Research Division, National Fisheries Research and Development Institute, Haean-ro 216, Gijang-eup, Gijang-gun, Busan 619-705, Korea. combikola@nfrdi.go.kr.
authors.forename: Dong-Gyun
authors.initials: DG
authors.lastname: Kim
authors.affiliation: Biotechnology Research Division, National Fisheries Research and Development Institute, Haean-ro 216, Gijang-eup, Gijang-gun, Busan 619-705, Korea. konghj@nfrdi.go.kr.
authors.forename: Hee Jeong
authors.initials: HJ
authors.lastname: Kong
authors.affiliation: Biotechnology Research Division, National Fisheries Research and Development Institute, Haean-ro 216, Gijang-eup, Gijang-gun, Busan 619-705, Korea. wjkim@nfrdi.go.kr.
authors.forename: Woo-Jin
authors.initials: WJ
authors.lastname: Kim
authors.affiliation: Biotechnology Research Division, National Fisheries Research and Development Institute, Haean-ro 216, Gijang-eup, Gijang-gun, Busan 619-705, Korea. philaqua@nfrdi.go.kr.
authors.forename: Young Ju
authors.initials: YJ
authors.lastname: Jee
authors.affiliation: Biotechnology Research Division, National Fisheries Research and Development Institute, Haean-ro 216, Gijang-eup, Gijang-gun, Busan 619-705, Korea. ancm@nfrdi.go.kr.
authors.forename: Cheul Min
authors.initials: CM
authors.lastname: An
authors.affiliation: Department of Biotechnology, Pukyong National University, Busan 608-737, Korea. ngpark@pknu.ac.kr.
authors.forename: Nam Gyu
authors.initials: NG
authors.lastname: Park
authors.affiliation: Department of Food Science and Biotechnology, Kunsan National University, Korea. jungkileun@kunsan.ac.kr.
authors.forename: Jung-Kil
authors.initials: JK
authors.lastname: Seo
mesh_terms: D000209:Acute-Phase Proteins / Q000378:metabolism*; D000818:Animals; D000890:Anti-Infective Agents / Q000378:metabolism* / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000378:metabolism*; D001798:Blood Proteins / Q000378:metabolism*; D002176:Candida albicans / Q000187:drug effects; D002352:Carrier Proteins / Q000378:metabolism*; D005432:Flounder / Q000378:metabolism*; D006090:Gram-Negative Bacteria / Q000187:drug effects; D006094:Gram-Positive Bacteria / Q000187:drug effects; D008562:Membrane Glycoproteins / Q000378:metabolism*; D008567:Membranes, Artificial; D010446:Peptide Fragments / Q000378:metabolism* / Q000494:pharmacology*; D017433:Protein Structure, Secondary; D000099231:Lipopolysaccharide-Binding Protein
chemical_list: D000209:Acute-Phase Proteins; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins; D002352:Carrier Proteins; D008562:Membrane Glycoproteins; D008567:Membranes, Artificial; D010446:Peptide Fragments; D000099231:Lipopolysaccharide-Binding Protein; C021623:bactericidal permeability increasing protein