Protein adductomics: Analytical developments and applications in human biomonitoring

George W. Preston, David H. Phillips*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

10 Citations (Scopus)


Proteins contain many sites that are subject to modification by electrophiles. Detection and characterisation of these modifications can give insights into environmental agents and endogenous processes that may be contributing factors to chronic human diseases. An untargeted approach, utilising mass spectrometry to detect modified amino acids or peptides, has been applied to blood proteins haemoglobin and albumin, focusing in particular on the N-terminal valine residue of haemoglobin and the cysteine-34 residue in albumin. Technical developments to firstly detect simultaneously multiple adducts at these sites and then subsequently to identify them are reviewed here. Recent studies in which the methods have been applied to biomonitoring human exposure to environmental toxicants are described. With advances in sensitivity, high-throughput handling of samples and robust quality control, these methods have considerable potential for identifying causes of human chronic disease and of identifying individuals at risk.

Original languageEnglish
Article number29
Issue number2
Publication statusPublished - 25 May 2019


  • Albumin
  • Biomarkers
  • Haemoglobin
  • Mass spectrometry
  • Protein adducts


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