New platform could transform protein research
A new platform for photoinduced-crosslinking could transform protein research.
Leading academics at the Astbury Centre for Structural Molecular Biology have significantly advanced a method for studying the interactions of proteins, which they say should transform research in this area.
Professor Sheena Radford, Director of the Centre, and a Fellow of the Royal Society, and colleague Professor Andrew Wilson, from the School of Chemistry at Leeds, have led the creation of a new platform for photoinduced-crosslinking.
Professor Wilson said:
Significant progress has been made in the development of methods for protein crosslinking, a key armament in the toolbox of methods used to study protein complexes and their formation.
Our new approach provides a route to study protein complexes and their role in fundamental biological processes within a more compatible time scale.
Professor Radford added:
The scientific community in the UK is among the best equipped in the world already for studying the interactions of proteins, thanks to existing methods like nuclear magnetic resonance, cryo-electron microscopy and x-ray crystallography. But where these methods are not feasible, our new approach could be used to great effect, and is uniquely suited to the study of rare, transient or dynamic complexes.
The eight strong research team, including chemists, structural biologists and engineers have published details of their method in the journal Angewandte Chemie.
Their study describes two new chemical crosslinking mass spectrometry (XL-MS) reagents and a workflow that enables crosslink identification for both well-defined and dynamic protein-protein interactions through photoinduced-crosslinking.
With the XL-MS reagents and a bespoke UV LED irradiation platform the team achieved a maximum crosslinking yield in 10 seconds– about 120 times faster when compared to using conventional mercury lamps for photocrosslinking.
The team have signed a non-exclusive licence to sell the new XL-MS reagents through Redbrick Molecular, so they can be used by research groups worldwide.
The University of Leeds has a strong track record of commercialising research and building links with industry. In addition to the commercialisation of individual research outcomes, the University has 200-plus collaborative research projects with business investors, enabling the University to achieve maximum impact from its research, promote private enterprise and enhance public benefit.
The paper Rapid Mapping of Protein Interactions Using Tag‐Transfer Photocrosslinkers is available on Angewandte Chemie (DOI: 10.1002/anie.201809149)
Redbrick Molecular Ltd
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