J. Adam Hendricks, Nigel Beaton*, Alexey Chernobrovkin, Eric Miele, Ghaith M. Hamza, Piero Ricchiuto, Ronald C. Tomlinson, Tomas Friman, Cassandra Borenstain, Bernard Barlaam, Sudhir Hande, Michelle L. Lamb, Chris De Savi, Rick Davies, Martin Main, Joakim Hellner, Kristina Beeler, Yuehan Feng, Roland Bruderer, Lukas Reiter, Daniel Martinez Molina*, and M. Paola Castaldi*. American Chemical Society’s Chemical Biology Journal.
The publication shows how orthogonal proteomics approaches can be applied to quantitatively profile the selectivity of a new compound. Biognosys’ proprietary Limited Proteolysis Mass Spectrometry (LiP-MS) technology was used to screen the entire proteome and identify potential targets via structural alterations. In addition to target identification, by exploiting the technology’s peptide-level resolution – a unique feature of the approach – we could also identify the putative binding site of the CDK inhibitor. In this way, LiP-MS enabled the target identification, binding affinity estimation, and binding site localization of the analyzed compound.