About this Biochemistry, Genetics and Molecular Biology article
Antibacterial Activity of Bactenecin 5 Fragments and Their Interaction with Phospholipid Membranes by Yoko Tokunaga; Takuro Niidome; Tomomitsu Hatakeyama; Haruhiko Aoyagi is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
## Abstract Bactenecin 5 (Bac 5) is an antibacterial 43mer peptide isolated from bovine neutrophils. It consists of an Arg‐rich __N__‐terminal region and successive repeats of Arg‐Pro‐Pro‐Ile (or Phe). We synthesized Bac 5~1‐23~ and several related peptides to clarify the roles these regions play in antibacterial activity. An assay of antibacterial activity revealed that such activity requires the presence of Arg residues at or near the __N__‐terminus, as well as a chain length exceeding 15 residues. None of the peptides exhibited haemolytic activity. Polyproline II‐like CD curves were observed for most of the peptides. Measurements of the membrane perturbation and fusion indicated that the perturbation and fusogenic activities of the peptides were, generally, parallel to their antibacterial activities. Amino acid substitution in the repeating region had some effect on antibacterial activity. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd.
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- Author
- Yoko Tokunaga; Takuro Niidome; Tomomitsu Hatakeyama; Haruhiko Aoyagi
- Publisher
- John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 1075-2617)
- Published
- 2001
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)