Analysis of the modification site in a small molecule-modified peptide by ion trap/time-of-flight hybrid mass spectrometry.
Ion trap/time-of-flight hybrid mass spectrometers are powerful tools for the detailed structural analysis of modified peptides. We have analyzed Met-Lys-bradykinin modified with deoxycholate at the amino-terminus or the epsilon-amino group as model peptides. These two modified peptides produced fragment ions with the same nominal but different exact masses in tandem mass spectrometry with low-energy collision-induced dissociation. Accurate high-resolution analysis coupled with MS(3) allowed us to distinguish the deoxycholate modification sites in the modified peptides.
Mano
Nariyasu
N
Graduate School of Pharmaceutical Sciences, Tohoku University, Aobayama, Aoba-ku, Sendai, 980-8578, Japan.
Kamota
Mio
M
Inohana
Yusuke
Y
Yamaguchi
Shin-Ichi
S
Goto
Junichi
J
D001665:Binding Sites; D001920:Bradykinin / Q000737:chemistry*; D003840:Deoxycholic Acid / Q000737:chemistry*; D008239:Lysine / Q000737:chemistry*; D008715:Methionine / Q000737:chemistry*; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D010455:Peptides; D003840:Deoxycholic Acid; D008715:Methionine; D008239:Lysine; D001920:Bradykinin