We have analyzed peptides, proteins, and protein-drug complexes through surface-assisted laser desorption/ionization mass spectrometry (SALDI-MS) using HgTe nanostructures as matrixes. We investigated the effects of several parameters, including the concentration of the HgTe nanostructures, the pH of the buffer, and the concentration of salt, on the performance of this system. When HgTe nanostructures are used as matrixes, [M + H](+) ions were the dominant signals. Relative to other commonly used nanomaterials, HgTe nanostructures provided lower background signals from metal clusters, fewer fragment ions, less interference from alkali-adducted analyte ions, and a higher mass range (up to 150,000 Da). The present approach provides limits of detection for angiotensin I and bovine serum albumin of 200 pM and 14 nM, respectively, with great reproducibility (RSD: <25%). We validated the applicability of this method through the detections of (i) the recombinant proteins that were transformed in E. coli, (ii) the specific complex between bovine serum albumin and l-tryptophan, and (iii) a carbonic anhydrase-acetazolamide complex. Our results suggest that this novel and simple SALDI-MS approach using HgTe nanostructures as matrixes might open several new ways for proteomics and the analysis of drug-protein complexes.
Surface-assisted laser desorption/ionization mass spectrometry (SALDI-MS) is applied to provide strong evidence for the chemical reactions of functionalized gold nanoparticles (Au NPs) with analytes--Hg(2+) ions induced MPA-Au NPs aggregation in the presence of 2,6-pyridinedicarboxylic acid (PDCA) and H(2)O(2) induced fluorescence quenching of 11-MUA-Au NDs. PDCA-Hg(2+)-MPA coordination is responsible for Au NPs aggregation, while the formation of 11-MUA disulfide compounds that release into the bulk solution is responsible for H(2)O(2)-induced fluorescence quenching. In addition to providing information about the chemical structures, SALDI-MS is also selective and sensitive for the detection of Hg(2+) ions and H(2)O(2). The limits of detection (LODs) for Hg(2+) ions and H(2)O(2) by SALDI-MS were 300 nM and 250 microM, respectively. The spot-to-spot variations in the two studies were both less than 18% (50 sample spots). Our results reveal that SALDI-MS can be used to study analyte-induced changes in the surface properties of nanoparticles.
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