title: Targeted engineering of the antibacterial peptide apidaecin, based on an in vivo monitoring assay system.
abstract: Seven mutant forms of the antibacterial peptide apidaecin with increased activity were created by combinatorial mutagenesis targeted to the three N-terminal amino acid residues that had previously been identified as a nonessential region. An in vitro MIC assay revealed that the amino acid substitutions in the functionally variable region were effective in improving differential activity toward the four gram-negative bacteria tested, while a gram-positive bacterium was unaffected.
authors.affiliation: Division of Biotechnology and Macromolecular Chemistry, Graduate School of Engineering, Hokkaido University, N13W8, Kita-ku, Sapporo-shi, Hokkaido 060-8628, Japan. staguchi@eng.hokudai.ac.jp
authors.forename: Seiichi
authors.initials: S
authors.lastname: Taguchi
authors.forename: Kensuke
authors.initials: K
authors.lastname: Mita
authors.forename: Kenta
authors.initials: K
authors.lastname: Ichinohe
authors.forename: Shigeki
authors.initials: S
authors.lastname: Hashimoto
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution / Q000235:genetics; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000235:genetics* / Q000494:pharmacology*; D019020:Directed Molecular Evolution; D006090:Gram-Negative Bacteria / Q000187:drug effects; D006094:Gram-Positive Bacteria / Q000187:drug effects; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D016296:Mutagenesis; D020125:Mutation, Missense
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; C061361:apidaecin