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Antimicrobial activity of peptides derived from olive flounder lipopolysaccharide binding protein/bactericidal permeability-increasing protein (LBP/BPI).

Nam BH, Moon JY, Park EH, Kim YO, Kim DG, Kong HJ, Kim WJ, Jee YJ, An CM, Park NG, Seo JK - Mar Drugs (2014)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Biotechnology 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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Bacterial killing kinetics of ofLBP analog peptides and piscidin 1 against Bacillus subtilis KCTC1021 (a) and Escherichia coli ML35p (b). Bacteria were incubated in the presence of 1× or 5× MEC of ofLBP analog peptides or piscidin 1. Control samples did not contain a peptide.
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marinedrugs-12-05240-f003: Bacterial killing kinetics of ofLBP analog peptides and piscidin 1 against Bacillus subtilis KCTC1021 (a) and Escherichia coli ML35p (b). Bacteria were incubated in the presence of 1× or 5× MEC of ofLBP analog peptides or piscidin 1. Control samples did not contain a peptide.

Mentions: To evaluate the inhibition mode of analogs, a killing kinetic study was performed against B. subtilis KCTC1021 and E. coli ML35p at their MECs and at five times their MECs (Figure 3). ofLBP 4N was not studied due to lack of activity against the two bacterial species used in this report. Analogs (excluding ofLBP 6A) did not kill the two bacterial strains at all tested concentrations. However, ofLBP 6A and piscidin 1 rapidly killed B. subtilis KCTC1021 within 10 min at the 5× MEC and within 40 min at the 1× MEC. To confirm the target site of antimicrobial activity, a killing kinetic study was performed against E. coli ML35p at its MEC and at five times its MEC. ofLBP 6A and piscidin 1 did not kill E. coil ML35p at the 1× MEC. However, ofLBP 6A and piscidin 1 killed this strain within 60 and 40 min, respectively, at the 5× MEC. These killing kinetic studies indicated that the inhibition mode of ofLBP 6A on the two bacteria is bactericidal rather than bacteriostatic, but that other analogs function through bacteriostatic processes. Similar to ofLBP 6A, piscidin 1 acted through a bactericidal process.


Antimicrobial activity of peptides derived from olive flounder lipopolysaccharide binding protein/bactericidal permeability-increasing protein (LBP/BPI).

Nam BH, Moon JY, Park EH, Kim YO, Kim DG, Kong HJ, Kim WJ, Jee YJ, An CM, Park NG, Seo JK - Mar Drugs (2014)

Bacterial killing kinetics of ofLBP analog peptides and piscidin 1 against Bacillus subtilis KCTC1021 (a) and Escherichia coli ML35p (b). Bacteria were incubated in the presence of 1× or 5× MEC of ofLBP analog peptides or piscidin 1. Control samples did not contain a peptide.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4210897&req=5

marinedrugs-12-05240-f003: Bacterial killing kinetics of ofLBP analog peptides and piscidin 1 against Bacillus subtilis KCTC1021 (a) and Escherichia coli ML35p (b). Bacteria were incubated in the presence of 1× or 5× MEC of ofLBP analog peptides or piscidin 1. Control samples did not contain a peptide.
Mentions: To evaluate the inhibition mode of analogs, a killing kinetic study was performed against B. subtilis KCTC1021 and E. coli ML35p at their MECs and at five times their MECs (Figure 3). ofLBP 4N was not studied due to lack of activity against the two bacterial species used in this report. Analogs (excluding ofLBP 6A) did not kill the two bacterial strains at all tested concentrations. However, ofLBP 6A and piscidin 1 rapidly killed B. subtilis KCTC1021 within 10 min at the 5× MEC and within 40 min at the 1× MEC. To confirm the target site of antimicrobial activity, a killing kinetic study was performed against E. coli ML35p at its MEC and at five times its MEC. ofLBP 6A and piscidin 1 did not kill E. coil ML35p at the 1× MEC. However, ofLBP 6A and piscidin 1 killed this strain within 60 and 40 min, respectively, at the 5× MEC. These killing kinetic studies indicated that the inhibition mode of ofLBP 6A on the two bacteria is bactericidal rather than bacteriostatic, but that other analogs function through bacteriostatic processes. Similar to ofLBP 6A, piscidin 1 acted through a bactericidal process.

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Biotechnology 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.

Show MeSH
Related in: MedlinePlus