4.7 Review

Peptidomics: A Review of Clinical Applications and Methodologies

Journal

JOURNAL OF PROTEOME RESEARCH
Volume 20, Issue 8, Pages 3782-3797

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.jproteome.1c00295

Keywords

peptidomics; mass spectrometry; clinical analysis

Funding

  1. iCASE studentship from the BBSRC
  2. LGC
  3. MRC [MRC_MC_UU_12012/3, MR/M009041/1]
  4. Wellcome Trust [220271/Z/20/Z]
  5. MRC [MR/M009041/1] Funding Source: UKRI
  6. Wellcome Trust [220271/Z/20/Z] Funding Source: Wellcome Trust

Ask authors/readers for more resources

Improvements in LC and MS instrumentation have enhanced proteomic and metabolomic analysis, but there has been less focus on detecting and quantifying small bioactive peptides. It is important to preserve the structure of processed peptide products to prevent misidentification and consider the stability of peptides in biological matrices when developing methods to study them. Bioinformatic analysis of peptidomics data sets should include specific post-translational modifications critical for the function of bioactive peptides.
Improvements in both liquid chromatography (LC) and mass spectrometry (MS) instrumentation have greatly enhanced proteomic and small molecule metabolomic analysis in recent years. Less focus has been on the improved capability to detect and quantify small bioactive peptides, even though the exact sequences of the peptide species produced can have important biological consequences. Endogenous bioactive peptide hormones, for example, are generated by the targeted and regulated cleavage of peptides from their prohormone sequence. This process may indude organ specific variants, as proglucagon is converted to glucagon in the pancreas but glucagon-like peptide-1 (GLP-1) in the small intestine, with glucagon raising, whereas GLP-1, as an incretin, lowering blood glucose. Therefore, peptidomics work-flows must preserve the structure of the processed peptide products to prevent the misidentification of ambiguous peptide species. The poor in vivo and in vitro stability of peptides in biological matrices is a major factor that needs to be considered when developing methods to study them. The bioinformatic analysis of peptidomics data sets requires the indusion of specific post-translational modifications, which are critical for the function of many bioactive peptides. This review aims to discuss and contrast the various extraction, analytical, and bioinformatics approaches used for human peptidomics studies in a multitude of matrices.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available