These authors contributed equally to this work.
Linear bactenecin analogs with cell selectivity and anti-endotoxic activity
Article first published online: 29 OCT 2012
Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.
Journal of Peptide Science
Volume 18, Issue 12, pages 740–747, December 2012
How to Cite
Hai Nan, Y., Jacob, B., Kim, Y. and Yub Shin, S. (2012), Linear bactenecin analogs with cell selectivity and anti-endotoxic activity. J. Peptide Sci., 18: 740–747. doi: 10.1002/psc.2460
- Issue published online: 13 NOV 2012
- Article first published online: 29 OCT 2012
- Manuscript Accepted: 21 SEP 2012
- Manuscript Revised: 29 AUG 2012
- Manuscript Received: 24 MAY 2012
- linear bactenecin analogs;
- cell selectivity;
- anti-endotoxin activity;
- serum stability
Bactenecin (Bac) is a 12-residue disulfide-linked antimicrobial peptide isolated from the granules of bovine neutrophils. In this study, to develop novel linear Bac analogs with cell selectivity and anti-endotoxic activity, we designed and synthesized a series of linear Bac analogs with amino acid substitution in Cys3,11 and/or Val6,7 of Bac. Among Bac analogs, some analogs (Bac-W, Bac-KW, Bac-L, Bac-KL, Bac-LW, and Bac-KLW) with higher hydrophobicity showed the amalgamated property of cell selectivity and anti-endotoxic activity. Furthermore, Bac-W, Bac-KW, Bac-LW, and Bac-KLW showed serum stability comparable with that of disulfide-bonded Bac. Therefore, these Bac analogs (Bac-W, Bac-KW, Bac-LW, and Bac-KLW) can serve as promising antibiotics for the development of therapeutic agents for treatment against endotoxic shock and bacterial infection. In addition, our results suggest that a little increase in hydrophobicity may be responsible for the decreased cell selectivity of the multiple Arg-containing peptides (Bac-W, Bac-L, and Bac-LW) over the multiple Lys-containing peptides (Bac-KW, Bac-KL, and Bac-KLW). Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.