Open AccessSolvent-free MALDI-MS for the analysis of biological samples via a mini-ball mill approach
Author(s) -
Sarah Trimpin,
Max L. Deinzer
Publication year - 2005
Publication title -
journal of the american society for mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.961
H-Index - 127
eISSN - 1879-1123
pISSN - 1044-0305
DOI - 10.1016/j.jasms.2004.12.014
Subject(s) - chemistry , chromatography , analyte , sample preparation , solvent , matrix assisted laser desorption/ionization , ball mill , matrix (chemical analysis) , ammonium acetate , peptide , grinding , analytical chemistry (journal) , biochemistry , organic chemistry , high performance liquid chromatography , desorption , chemical engineering , adsorption , mechanical engineering , engineering
An efficient, low sample load mini-ball mill (MBM) sample preparation procedure was developed for solvent-free MALDI analysis of peptides and proteins. Picomole sample amounts can be handled conveniently, with 30 s grinding times being sufficient. Matrix purity and molar analyte/matrix ratios are not as critical as with methods employing solvent. Ammonium salt is employed for protonation of the peptide and suppression of sodiation. This strategy allows for peptide mapping and other biochemical manipulations to be performed prior to MBM sample preparation and mass analysis. The analysis of bovine serum albumin (66 kDa) yielded good results, indicating that higher molecular weight proteins are accessible. A semi-solvent-free strategy by the MBM sample preparation method is also described.