Guanidination of tryptic peptides without desalting for matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry analysis.

ABSTRACT: Derivatizations that enhance mass spectral quality often require desalting, which presents as a bottleneck in matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF MS)-proteomics. Guanidination, which converts lysine to homoarginine, an arginine analogue, can increase detection of those peptides 5-15-fold. Our aim was to improve guanidination by using a novel reagent, O-methylisourea-freebase. In a simple reaction, interfering salts were removed prior to guanidination. Freebase preparation took about 30 min and could be applied to samples all at once as opposed to desalting samples one-by-one for 5 min each. For freebase guanidinated BSA tryptic peptides, more than 6-times the peptides were observed relative to tryptic peptides or those guanidinated with t

SUBMITTER: Baker MR 

PROVIDER: S-EPMC3820968 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature