Location of the three disulfide bonds in an antimicrobial peptide from Amaranthus caudatus using mass spectrometry.
The disulfide bridge pairing of Ac-AMP2, a 30-residue peptide isolated from the seeds of Amaranthus caudatus, is determined using a fast method involving enzymatic fragmentation followed by identification of the fragments with FAB mass spectrometry. The results confirm the location of the three disulfide bridges as previously established by NMR spectroscopy and molecular modelling.
el Bouyoussfi
M
M
Organic Chemistry Department, Vrije Universitet Brussel, Belgium.
Laus
G
G
Verheyden
P
P
Wyns
L
L
Tourwe
D
D
Van Binst
G
G
D000595:Amino Acid Sequence; D000890:Anti-Infective Agents / Q000737:chemistry*; D004220:Disulfides; D010450:Endopeptidases; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D012639:Seeds / Q000737:chemistry*; D016339:Spectrometry, Mass, Fast Atom Bombardment / Q000379:methods
D000890:Anti-Infective Agents; D004220:Disulfides; D010446:Peptide Fragments; D010455:Peptides; D010450:Endopeptidases