PT  - JOURNAL ARTICLE
AU  - Huiyan Li
AU  - Robert Popp
AU  - Christoph H. Borchers
TI  - Affinity-mass spectrometric technologies for quantitative proteomics in biological fluids
AID  - 10.1101/114751
DP  - 2017 Jan 01
TA  - bioRxiv
PG  - 114751
4099  - http://biorxiv.org/content/early/2017/03/08/114751.short
4100  - http://biorxiv.org/content/early/2017/03/08/114751.full
AB  - 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.