Comparative analyses of different surfactants on matrix-assisted laser desorption/ionization mass spectrometry peptide analysis

Abstract

Matrix-assisted Laser Desorption/Ionization Mass Spectrometry (MALDI-MS) has been extensively used for proteomics and peptidomics analysis. Nevertheless, these analyses, when focused on low molecular mass proteins, show some limitation due to background interference from surfactant ions. Surfactants are routinely used as a solubilizing or denaturing agents for proteins and peptides. In this report, an evaluation and further comparison of the effects of an ionic surfactant, Sodium Dodecyl Sulfate (SDS), and a non-ionic surfactant, tergitol, on MALDI-MS analyses of the amphipathic peptides, angiotensin and bradykinin, were carried out. At concentrations ≥ 10 mmol L⁻¹, SDS deteriorates the MALDI spectral quality by reducing the signal and intensity of the analyte ions. In particular, it affects the hydrophobic peptide where the signal of surfactant-interfering ions suppresses the analyte ion signal. Whereas, the non-ionic surfactant, tergitol, improves the MALDI-MS analysis of peptide mixtures or hydrophobic peptides by reducing interference from the surfactant itself in positive ion mode analysis. Three-dimensional molecular modeling of two different peptides in complex to tergitol NP-40 and SDS were conducted in order to explain the molecular effects of both agents. In summary, while SDS must be removed from the sample solution to avoid interference of ions from SDS and suppression of analyte ion signal, tergitol at low concentrations may be used as an additive with sample solution for MALDI-MS analysis of peptides. Finally, molecular modeling analyses associated with docking were used in order to explain experimental biochemical data.