Determination of the disulfide array in sapecin, an antibacterial peptide of Sarcophaga peregrina (flesh fly).
Sapecin is a 40-residue peptide containing 6 half-cystine residues. The disulfide structure of sapecin was determined by sequencing cystine-containing peptides obtained by digesting sapecin with thermolysin. Results showed that sapecin has a vortical structure fixed by 3 disulfide bonds between cysteine residues 3 and 30, 16 and 36, and 20 and 38, respectively, and that these disulfide bonds are essential for its antibacterial activity.
Kuzuhara
T
T
Faculty of Pharmaceutical Sciences, University of Tokyo.
Nakajima
Y
Y
Matsuyama
K
K
Natori
S
S
D000595:Amino Acid Sequence; D000818:Animals; D000890:Anti-Infective Agents / Q000032:analysis*; D002478:Cells, Cultured; D002851:Chromatography, High Pressure Liquid; D003545:Cysteine / Q000032:analysis; D004175:Diptera / Q000032:analysis*; D004220:Disulfides / Q000032:analysis*; D004229:Dithiothreitol; D007301:Insect Hormones / Q000032:analysis*; D019476:Insect Proteins; D008969:Molecular Sequence Data; D012995:Solubility; D013820:Thermolysin
D000890:Anti-Infective Agents; D004220:Disulfides; D007301:Insect Hormones; D019476:Insect Proteins; C057638:sapecin protein, Sarcophaga; D013820:Thermolysin; D003545:Cysteine; D004229:Dithiothreitol