New Method for Profiling Cysteine-Reacting Fragments in Proteomics
Author Information
Author(s): George S. Biggs, Emma E. Cawood, Aini Vuorinen, William J. McCarthy, Harry Wilders, Ioannis G. Riziotis, Antonie J. van der Zouwen, Jonathan Pettinger, Luke Nightingale, Peiling Chen, Andrew J. Powell, David House, Simon J. Boulton, J. Mark Skehel, Katrin Rittinger, Jacob T. Bush
Primary Institution: The Francis Crick Institute, London, UK
Hypothesis
Can a high-throughput, label-free chemoproteomics platform effectively identify ligand-protein interactions across the human proteome?
Conclusion
The study successfully developed a high-throughput platform that identified over 400 ligand-protein interactions using cysteine-reactive fragments.
Supporting Evidence
- The platform identified >400 ligand-protein interactions from 80 screened fragments.
- Data completeness was high, with two-thirds of peptides detected in ≥75% of samples.
- Over 8000 proteins were detected, representing ~40% of the human proteome.
Takeaway
Researchers created a new way to find how small molecules interact with proteins in our bodies, which can help in making new medicines.
Methodology
The study used a label-free quantification proteomics platform to profile cysteine-reactive fragments against the native proteome, employing data-independent acquisition for high-throughput screening.
Limitations
The platform achieves ~40% coverage of the proteome but less than 15% of the entire cysteinome.
Statistical Information
P-Value
p<0.05
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website