title: Design, Characterization, and Antimicrobial Activity of a Novel Antimicrobial Peptide Derived from Bovine Lactophoricin.
abstract: Lactophoricin (LPcin), which is a part of proteose peptone isolated from bovine milk, is a cationic amphipathic α-helical antimicrobial peptide. Its truncated variants and mutated analogs were designed and their antimicrobial activities were evaluated by using various assays, like broth dilution methods and disk diffusion methods as well as hemolysis assay. Three analogs, LPcin-C8 (LPcin-YK1), LPcin-T2&6W (LPcin-YK2), and LPcin-T2&6W-C8 (LPcin-YK3), which showed better antibiotic activities than LPcin, were selected. Their secondary structures were also characterized by using CD spectropolarimetry. These three analogs of LPcin could be used as an alternative source of powerful antibacterial agents.
authors.affiliation: Department of Chemistry, Hankuk University of Foreign Studies, Yongin 17035, Republic of Korea.
authors.forename: Ji-Sun
authors.initials: JS
authors.lastname: Kim
authors.affiliation: Department of Chemistry, Hankuk University of Foreign Studies, Yongin 17035, Republic of Korea.
authors.forename: Ji-Ho
authors.initials: JH
authors.lastname: Joeng
authors.affiliation: Department of Chemistry, Hankuk University of Foreign Studies, Yongin 17035, Republic of Korea.
authors.forename: Yongae
authors.initials: Y
authors.lastname: Kim
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D001419:Bacteria / Q000187:drug effects; D002364:Caseins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D002413:Cations, Divalent / Q000737:chemistry / Q000494:pharmacology; D002417:Cattle; D002460:Cell Line / Q000187:drug effects; D002470:Cell Survival; D002522:Chlorocebus aethiops; D006224:Cricetinae; D052978:Disk Diffusion Antimicrobial Tests / Q000379:methods; D006461:Hemolysis; D006801:Humans; D020128:Inhibitory Concentration 50; D051379:Mice; D008826:Microbial Sensitivity Tests; D008894:Milk Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D041681:NIH 3T3 Cells / Q000187:drug effects; D010446:Peptide Fragments / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D017433:Protein Structure, Secondary; D013053:Spectrophotometry / Q000379:methods; D013329:Structure-Activity Relationship; D014709:Vero Cells / Q000187:drug effects
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D002364:Caseins; D002413:Cations, Divalent; D008894:Milk Proteins; D010446:Peptide Fragments; C018135:proteose-peptone
keywords: Bovine lactophoricin; antimicrobial activity; antimicrobial peptide; cationic amphipathic peptides; engineered analogs