Targeted engineering of the antibacterial peptide apidaecin, based on an in vivo monitoring assay system.
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.
Taguchi
Seiichi
S
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
Mita
Kensuke
K
Ichinohe
Kenta
K
Hashimoto
Shigeki
S
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
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; C061361:apidaecin