Instability of side-chain protecting groups during MALDI-TOF mass spectrometry of peptide fragments.
Matrix-assisted laser desorption and ionization time-of-flight mass spectrometry (MALDI-TOF MS), a well-suited method for the characterization of peptides and proteins, was used for analysis of protected peptide fragments. It is shown that acidic matrices, e.g. 2,5-dihydroxybenzoic acid, frequently used in MALDI-TOF MS of peptides, causes partial cleavage of acid-labile side-chain protecting groups. Because this effect is strongly related to the matrix used, the observed deprotection can be avoided by choosing an appropriate matrix such as 2,4,6-trihydroxyacetophenone or 2-amino-5-nitropyridine. The advantage of neutral matrix compounds for MALDI-TOF analysis of protected peptides is clearly demonstrated, confirming the potential of MALDI-TOF mass spectrometry.
Schmidt
M
M
Institute of Molecular Pharmacology, Berlin, Germany.
Krause
E
E
Beyermann
M
M
Bienert
M
M
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D010446:Peptide Fragments