Nanoporous aluminum oxide layers, grown by anodization of aluminum thin films on glass and then sputter-coated with gold, were used to study the effects of the thin-film structural parameters on laser desorption/ionization (LDI) mass spectrometry (MS) of peptides. Variation of MS signal intensity was examined as a function of alumina pore depth, pore width, and gold layer thickness. Peptide molecular ion intensity was optimal with porous alumina formed from aluminum films of approximately 600-nm thickness; thinner or thicker films gave significantly lower signals. Signals decreased when pore sizes were increased beyond the as-formed width of approximately 100 nm. The MS signal also varied with the thickness of the sputtered gold layer with an optimum thickness being approximately 90 nm. The results of these studies provide values for empirical optimization of LDI MS performance as well as potential clues to the LDI mechanism.
Exosomes are nano-sized extracellular vesicles that serve as a communications system between cells and has shown tremendous promise as liquid biopsy biomarkers in diagnostic, prognostic, and even therapeutic use in...
A novel matrix-free LDI MS platform using a thin film of patterned nanostructured gold, capped with methyl-and carboxy-terminated self assembled monolayers (SAM) is presented. Calibration on the matrix-free LDI surface was performed using a peptide standard mixture available for MALDI analysis. MS analysis for limit of detection was performed using angiotensin I peptide. Peptide fragments from standard protein digests of bovine serum albumin, bovine catalase and bovine lactoperoxidase were used to carry out peptide mass fingerprinting analysis. Sequence coverage of each protein digest and the number of detected peptide fragments were compared with conventional MALDI MS on a standard MALDI plate. Versatility of the nanostructured gold LDI substrate is illustrated by performing MS analysis on a protein digest using different enzymes and by small molecule MS analysis.
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