Journal
CHEMICAL SCIENCE
Volume 12, Issue 4, Pages 1451-1457Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0sc05330a
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Funding
- National Key R&D Program of China [2016YFF0200504]
- National Natural Science Foundation of China [91853101, 21675152]
- Original Innovation Project of CAS [ZDBS-LY-SLH032]
- DICP [DICPI202007]
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Researchers developed a TILLRP strategy using mass spectrometry to probe the key lysine sites involved in the binding of SARS-CoV-2 S1 to ACE2, with significant alterations in lysine reactivities observed at the interface of S1-RBD during protein interactions.
Probing the conformational and functional hotspot sites within aqueous native protein complexes is still a challenging task. Herein, a mass spectrometry (MS)-based two-step isotope labeling-lysine reactivity profiling (TILLRP) strategy is developed to quantify the reactivities of lysine residues and probe the molecular details of protein-protein interactions as well as evaluate the conformational interventions by small-molecule active compounds. The hotspot lysine sites that are crucial to the SARS-CoV-2 S1-ACE2 combination could be successfully probed, such as S1 Lys(417) and Lys(444). Significant alteration of the reactivities of lysine residues at the interaction interface of S1-RBD Lys(386)-Lys(462) was observed during the formation of complexes, which might be utilized as indicators for investigating the S1-ACE2 dynamic recognition and intervention at the molecular level in high throughput.
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