Research Article
Chemical synthesis, characterization and activity of RK-1, a novel α-defensin-related peptide
Article first published online: 31 JAN 2000
DOI: 10.1002/(SICI)1099-1387(200001)6:1<19::AID-PSC230>3.0.CO;2-1
Copyright © European Peptide Society and John Wiley & Sons, Ltd.
Additional Information
How to Cite
Dawson, N. F., Craik, D. J., Mcmanus, A. M., Dashper, S. G., Reynolds, E. C., Tregear, G. W., Otvos Jr, L. and Wade, J. D. (2000), Chemical synthesis, characterization and activity of RK-1, a novel α-defensin-related peptide. J. Peptide Sci., 6: 19–25. doi: 10.1002/(SICI)1099-1387(200001)6:1<19::AID-PSC230>3.0.CO;2-1
Publication History
- Issue published online: 31 JAN 2000
- Article first published online: 31 JAN 2000
- Manuscript Accepted: 5 AUG 1999
- Manuscript Received: 2 AUG 1999
Funded by
- University of Queensland Travelling Scholarship
- National Health and Medical Research Council of Australia. Grant Number: 983001
- Abstract
- References
- Cited By
Keywords:
- antibacterial assay;
- α-defensin;
- disulfide bond assignment;
- Fmoc-solid phase peptide synthesis;
- 1H-NMR spectroscopy;
- mass spectroscopy;
- RK-1
Abstract
The 32-residue peptide, RK-1, a novel kidney-derived three disulfide-bonded member of the antimicrobial α-defensin family, was synthesized by the continuous flow Fmoc-solid phase method. The crude, cleaved and S-reduced linear peptide was both efficiently folded and oxidized in an acidic solution of aqueous dimethyl sulfoxide. Following purification of the resulting product, it was shown by a variety of analytical techniques, including matrix assisted laser desorption time of flight mass spectrometry, to possess a very high degree of purity. The disulfide bond pairing of the synthetic peptide was determined by 1H-NMR spectroscopy and confirmed to be a Cys1-Cys6, Cys2-Cys4, Cys3-Cys5 arrangement similar to other mammalian α-defensin peptides. The synthetic RK-1 was also shown to inhibit the growth of Escherichia coli type strain NCTC 10418. Copyright © 2000 European Peptide Society and John Wiley & Sons, Ltd.

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