Matrix-assisted laser desorption/ionization quadrupole time-of-flight mass spectrometry: an elegant tool for peptidomics

Proteomics. 2001 Jan;1(1):118-31. doi: 10.1002/1615-9861(200101)1:1<118::AID-PROT118>3.0.CO;2-1.


A Matrix-assisted laser desorption/ionization hybrid quadrupole orthogonal acceleration time-of-flight mass spectrometer was employed to acquire neuropeptide mass spectra, directly from neuropeptide secreting tissue deposited on the sample target, in the presence of dihydroxybenzoic acid as matrix. The cockroach corpus cardiacum served as model neuroendocrine tissue. Twelve neuropeptide ion peaks, with mass-to-charge ratio values ranging between 800 and 3,000 Da were selected for tandem mass spectrometry. All peptides below 1,600 Da could be fully sequenced; tandem mass spectrometry analysis of the remaining (three) largest peptides resulted in (limited) sequence tags, which, also due to unavailability of an appropriate neuropeptide structure database, did not allow complete structure elucidation.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cockroaches / chemistry
  • Cockroaches / genetics
  • Insect Proteins / genetics
  • Insect Proteins / isolation & purification
  • Molecular Sequence Data
  • Neuropeptides / genetics
  • Neuropeptides / isolation & purification*
  • Neurosecretory Systems / chemistry
  • Peptide Fragments / genetics
  • Peptide Fragments / isolation & purification
  • Proteome / genetics
  • Proteome / isolation & purification*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods*


  • Insect Proteins
  • Neuropeptides
  • Peptide Fragments
  • Proteome