Affinity-mass spectrometric technologies for quantitative proteomics in biological fluids

Huiyan Li, Robert Popp, Christoph H. Borchers

Research output: Contribution to journalReview articlepeer-review

18 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)80-88
Number of pages9
JournalTrAC - Trends in Analytical Chemistry
Publication statusPublished - 1 May 2017
Externally publishedYes


  • Affinity-mass spectrometry
  • Biomarkers
  • Immuno-enrichment
  • Limit of detection
  • Multiplexing
  • Protein quantification
  • Specificity
  • Throughput


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