Characterization of an N-acylated glucagon-like peptide-1 derivative by electron capture dissociation.
An N-acylated glucagon-like peptide 1 derivative was characterized by Fourier transform ion cyclotron resonance mass spectrometry. Both electron capture dissociation (ECD) and sustained off-resonance irradiation collisionally activated dissociation (SORI-CAD) were employed. While ECD revealed full sequence coverage, site of modification, branching point, structure of the palmitoylated modification, SORI-CAD produced less complete and more ambiguous information attributable to facile losses of the fatty acid group from both parent and fragments. Thus, ECD showed a superior characterization performance over SORI-CAD in analysis of N-acylated polypeptides.
Haselmann
Kim F
KF
Department of Chemistry, University of Southern Denmark, Odense, Denmark. kfh@chem.sdu.dk
Nielsen
Per F
PF
Zubarev
Roman A
RA
D000215:Acylation; D003924:Diabetes Mellitus, Type 2 / Q000188:drug therapy; D005934:Glucagon / Q000737:chemistry*; D052216:Glucagon-Like Peptide 1; D007004:Hypoglycemic Agents / Q000737:chemistry* / Q000627:therapeutic use; D010446:Peptide Fragments / Q000737:chemistry*; D011498:Protein Precursors / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*
D007004:Hypoglycemic Agents; D010446:Peptide Fragments; D011498:Protein Precursors; C501839:gamma-L-glutamoyl(Nalpha-hexadecanoyl)-R(34-7)GLP-1(37); D052216:Glucagon-Like Peptide 1; D005934:Glucagon