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Germany: ProteomeTools Library of the Human Proteome

| Editor: Alexander Stark

Researchers led by the Technical University of Munich (TUM) report on the synthesis of a library of more than 330,000 reference peptides representing essentially all canonical proteins of the human proteome. This research is a major milestone in the ProteomeTools project which aims at translating human proteome information into new molecular and digital tools with the potential for use in drug discovery, personalized medicine and life science research.

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Mathias Wilhelm (l.) and Professor Bernhard Küster (r.) in discussion about the ProteomeTools Peptide Library called PROPEL.
Mathias Wilhelm (l.) and Professor Bernhard Küster (r.) in discussion about the ProteomeTools Peptide Library called PROPEL.
(Source: Andreas Heddergott/ TUM)

Munich/Germany — In a manuscript published online in Nature Methods, ProteomeTools scientists report on the synthesis of a library of more than 330,000 reference peptides (termed Propel for ProteomeTools Peptide Library) representing essentially all canonical proteins of the human proteome. All peptides were analysed by multi-modal liquid chromatography-tandem mass spectrometry (LC-MS/MS), creating a compendium of millions of very high quality reference spectra (termed Prospect for ProteomeTools Spectrum Compendium). The study illustrates the utility of these reagents and data to verify protein identifications from sparse observations and to predict the behaviour of peptides during liquid chromatography and tandem mass spectrometry.

The consortium of TUM, JPT Peptide Technologies (JPT), SAP and Thermo Fisher Scientific has made the vast quantity of data freely available to the scientific community via the data analytics platform ProteomicsDB and the data repository Pride to enable scientists and to foster collaboration around the globe. Going forward, the ProteomeTools project will generate a further one million peptides and corresponding spectra with a focus on splice variants, cancer mutations and post-translational modifications such as phosphorylation, acetylation and ubiquitinylation.

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