Fast Radical Footprinting for Protein-Ligand Interaction Analysis

Metal ions, small organic molecules, peptides and small proteins are the ligands tested thus far. PLIMSTEX should be applicable to other ligands including nucleic acids and other proteins. PLIMSTEX should have utility for measuring affinities of proteins in complexes as well as alone, and if this works, it may be one of the few techniques that can probe interaction of a ligand with one protein that is interacting with others. 

A key future direction is expanding PLIMSTEX to provide a higher resolved view than the global view of the whole protein that is currently obtained. Digestion with pepsin followed by peptide analysis by MS and MS/MS should allow kinetics and titrations to be measured for portions of a protein, giving PLIMSTEX a view of the protein that currently emerges from NMR and X-ray methods. 

Fast Radical Footprinting for Protein-Ligand Interaction Analysis 

---