Antimicrobial Activity of Peptides Derived from Olive Flounder Lipopolysaccharide Binding Protein/Bactericidal Permeability-Increasing Protein (LBP/BPI)

• Main Authors: Bo-Hye Nam, Ji-Young Moon, Eun-Hee Park, Young-Ok Kim, Dong-Gyun Kim, Hee Jeong Kong, Woo-Jin Kim, Young Ju Jee, Cheul Min An, Nam Gyu Park, Jung-Kil Seo
• Format: Article
• Language: English
• Published: MDPI AG 2014-10-01
• Series: Marine Drugs
• Subjects: antimicrobial peptide; LPS-binding protein; bactericidal permeability-increasing protein; analogs; antimicrobial mechanism
• Online Access: http://www.mdpi.com/1660-3397/12/10/5240

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.