Chemical synthesis, characterization and activity of RK-1, a novel alpha-defensin-related peptide.
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.
Dawson
N F
NF
Howard Florey Institute of Experimental Physiology and Medicine, University of Melbourne, Parkville, Victoria, Australia.
Craik
D J
DJ
McManus
A M
AM
Dashper
S G
SG
Reynolds
E C
EC
Tregear
G W
GW
Otvos
L
L
Wade
J D
JD
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D023082:Defensins; D004926:Escherichia coli / Q000187:drug effects; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000378:metabolism*; D010452:Peptide Biosynthesis; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D017510:Protein Folding; D011506:Proteins / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D023084:alpha-Defensins
D023082:Defensins; D009842:Oligopeptides; D010455:Peptides; D011506:Proteins; C405106:RK-1 peptide; D023084:alpha-Defensins