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bioRxiv · 10.1101/114751

Affinity-mass spectrometric technologies for quantitative proteomics in biological fluids

Li, H.·Popp, R.·Borchers, C. H.
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Abstract

Proteins are the functional molecules in organisms and are therefore excellent biomarker candidates for a diversity of diseases. Immunoassays and mass spectrometry (MS) are two major technologies being used in proteomics; however, they either lack specificity or sensitivity. An emerging trend is to combine immunoassays with MS (which we call \"affinity-MS\"). This is an important milestone in quantitative proteomics, making it possible to measure low-abundance proteins with high specificity. The targeted enrichment and the assignment of mass-to-charge ratios to different molecules provide two selection criteria, making affinity-MS highly specific. Picogram-per-milliliter limits of detection have been obtained for many proteins. Furthermore, multiplexing capacity of >150 proteins has been achieved. This article reviews different formats of affinity-enrichment methods, and demonstrates how they are interfaced with both electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) MS. The pros and cons of these techniques are compared, and future prospectives are discussed.

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Li, H., Popp, R., Borchers, C. H.. 2017-03-08. Affinity-mass spectrometric technologies for quantitative proteomics in biological fluids. https://doi.org/10.1101/114751

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