Autor: |
N F, Dawson, D J, Craik, A M, McManus, S G, Dashper, E C, Reynolds, G W, Tregear, L, Otvos, J D, Wade |
Rok vydání: |
2000 |
Předmět: |
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Zdroj: |
Journal of peptide science : an official publication of the European Peptide Society. 6(1) |
ISSN: |
1075-2617 |
Popis: |
The 32-residue peptide, RK-1, a novel kidney-derived three disulfide-bonded member of the antimicrobial alpha-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 alpha-defensin peptides. The synthetic RK-1 was also shown to inhibit the growth of Escherichia coli type strain NCTC 10418. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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