Structural elucidation of minor components of peptidyl antibiotic P168s (leucinostatins) by tandem mass spectrometry.
Tandem mass spectrometry with a four-sector type mass spectrometer was used to elucidate the structures of minor components of the peptidyl antibiotic P168s (leucinostatins). As N-terminal fragments, ions by B-type cleavage were dominant, while V-type cleavages were observed along with X, Y, and Z types as C-terminal ions. The V-type ions were predominant in the cleavages of the amino terminals of leucyl and hydroxyleucyl residues. The structures of several minor components could be deduced from the tandem mass spectra.
Department of Agricultural Chemistry, University of Tokyo, Japan.
A
A
Isogai
J
J
Nakayama
S
S
Takayama
A
A
Kusai
A
A
Suzuki
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D023181:Antimicrobial Cationic Peptides; D001709:Biotechnology; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*
D000596:Amino Acids; D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D010455:Peptides; C008268:leucinostatin A