Solvent-free MALDI-MS for the analysis of biological samples via a mini-ball mill approach.
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.
Trimpin
Sarah
S
Department of Chemistry, Oregon State University, Corvallis, Oregon 97331, USA.
Deinzer
Max L
ML
D000818:Animals; D001779:Blood Coagulation Factors / Q000032:analysis*; D002417:Cattle; D045304:Cytochromes c / Q000032:analysis*; D008832:Microchemistry / Q000379:methods; D010449:Peptide Mapping / Q000379:methods; D012710:Serum Albumin, Bovine / Q000032:analysis*; D012997:Solvents / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D013678:Technology, Pharmaceutical
D001779:Blood Coagulation Factors; D012997:Solvents; D012710:Serum Albumin, Bovine; C031546:platelet factor 1; D045304:Cytochromes c