Improving the sensitivity of matrix-assisted laser desorption/ionization (MALDI) mass spectrometry by using...

Previous studies in our group have shown that the analyte signal in a matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS) experiment is strongly influenced by the binding interactions between the target surface and the analyte. Specifically, the analyte signal increases with decreases in surface binding affinity, which has been attributed to more unbound analyte being available for incorporation within the MALDI matrix. In this work, polyethylene glycol (PEG) was chemically grafted onto a polyurethane (PU) film to produce a MALDI target having reduced surface-protein binding affinity, and the effect of this modification on protein MALDI ion signals was investigated. The proteins myoglobin, lysozyme, and albumin were used to evaluate the PEG PU modified target as compared with a PU target and a commercial stainless steel target. It is shown that there are enhancements in the protein MALDI ion signals on the PEG PU modified target and that the limit of detection for these proteins is decreased by a factor of 2 to 6 in comparison with the unmodified PU and the commercial stainless steel targets.