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Antibacterial activity of bactenecin 5 fragments and their interaction with phospholipid membranes

✍ Scribed by Yoko Tokunaga; Takuro Niidome; Tomomitsu Hatakeyama; Haruhiko Aoyagi

Publisher
John Wiley and Sons
Year
2001
Tongue
English
Weight
190 KB
Volume
7
Category
Article
ISSN
1075-2617

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✦ Synopsis

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 Β© 2001 European Peptide Society and John Wiley & Sons, Ltd.

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