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Review
. 2015 Sep;36(9):579-86.
doi: 10.1016/j.tips.2015.05.009. Epub 2015 Jul 1.

Peptidomics for the discovery and characterization of neuropeptides and hormones

Elena V Romanova  1 , Jonathan V Sweedler  2
Affiliations
Review

Peptidomics for the discovery and characterization of neuropeptides and hormones

Elena V Romanova et al. Trends Pharmacol Sci. 2015 Sep.

Abstract

The discovery of neuropeptides as signaling molecules with paracrine or hormonal regulatory functions has led to trailblazing advances in physiology and fostered the characterization of numerous neuropeptide-binding G protein-coupled receptors (GPCRs) as potential drug targets. The impact on human health has been tremendous: approximately 30% of commercial drugs act via the GPCR pathway. However, about 25% of the GPCRs encoded by the mammalian genome still lack their pharmacological identity. Searching for the orphan GPCR endogenous ligands that are likely to be neuropeptides has proved to be a formidable task. Here we describe the mass spectrometry (MS)-based technologies and experimental strategies that have been successful in achieving high-throughput characterization of endogenous peptides in nervous and endocrine systems.

Keywords: bioinformatics; endogenous peptides; mass spectrometry; nervous system; quantitation; sequencing.

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Figures

Figure 1
Figure 1
A simplified flow chart showing (A) a general peptidomics workflow and (B) a strategy that helps to explain the wide variety of mass spectrometry platforms and for which experiments to use them.
Figure 2
Figure 2
Synergy of tools and resources in peptidomics research showing both (A) non-targeted approaches and (B) targeted approaches.
Figure 3
Figure 3
Bioinformatics approaches for MS-based peptide identification. Two categories of approaches are distinct: the database search approach depends on generating theoretical spectra in silico from protein sequences in a database and querying experimental spectra against those to find the closest matches; the de novo tag approach infers peptide sequence directly from experimental MS/MS data by calculating mass shifts between series of peptide fragment ions, and then aligns the tag to protein in the database. Unassigned de novo tags can be used to interrogate EST depositories or databases of homologous species.
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