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Chemical synthesis, characterization and activity of RK-1, a novel α-defensin-related peptide

✍ Scribed by Nicola F. Dawson; David J. Craik; Ailsa M. Mcmanus; Stuart G. Dashper; Eric C. Reynolds; Geoffrey W. Tregear; Laszlo Otvos Jr; John D. Wade

Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
141 KB
Volume
6
Category
Article
ISSN
1075-2617

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✦ Synopsis

The 32-residue peptide, RK-1, a novel kidney-derived three disulfide-bonded member of the antimicrobial h-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 1 H-NMR spectroscopy and confirmed to be a Cys 1 -Cys 6 , Cys 2 -Cys 4 , Cys 3 -Cys 5 arrangement similar to other mammalian h-defensin peptides. The synthetic RK-1 was also shown to inhibit the growth of Escherichia coli type strain NCTC 10418.

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