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The Bcr/Abl chimeric protein was captured by two antibodies, anti-Bcr on gold nanoparticles (AuNPs) and anti-Abl on a biochip, in a sandwich assay format. The presence of the Bcr/Abl in cells was then verified by amplified LDI-TOF MS signals, and relative amounts were quantified using AuNPs coated with deuterated alkanethiols as an internal standard.

In this report, we present a simple, cost effective, and less laborious method for the absolute and multiplexed quantification of surfacebound proteins using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) and the isotopelabeled internal standards (ISs).

We report a fast and sensitive method for the multiplexed detection of miRNAs by combining mass signal amplification and isotope-labeled signal reporter molecules. In our strategy, target miRNAs are captured specifically by immobilized DNAs on gold nanoparticles (AuNPs), which carry a large number of small molecules, called amplification tags (Am-tags), as the reporter for the detection of target miRNAs. For multiplexed detection, we designed and synthesized four Am-tags containing 0, 4, 8, 12 isotopes so that they had same molecular properties but different molecular weights. By observing the mass signals of the Am-tags on AuNPs decorated along with different probe DNAs, four types of miRNAs in a sample could be easily discriminated, and the relative amounts of these miRNAs could be quantified. The practicability of our strategy was further verified by measuring the expression levels of two miRNAs in HUVECs in response to different CuSO concentrations.

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