Covalent and non-covalent ligand-macromolecule interaction studies by mass spectrometry

This area of research concerns the identification and characterisation of ligands (covalent and non-covalent) of macromolecules, in particular proteins and nucleic acids, by means of diversified proteomics and mass spectrometry approaches, including high-resolution mass spectrometry (HMRS) in intact protein analysis (top-down approach) and shotgun proteomics (bottom-up approach). The technology has been applied in recent years not only to the search for new ligands (covalent and non-covalent) but also to the study of the mechanism of protein haptenation.

Pubblicazioni

• Baron G., Borella S., Della Vedova L., Vittorio S., Vistoli G., Carini M., Aldini G., Altomare A. An integrated metabolomic and proteomic approach for the identification of covalent inhibitors of the main protease (Mpro) of SARS-COV-2 from crude natural extracts. Talanta. 2023 Jan 15;252:123824. doi: 10.1016/j.talanta.2022.123824.
• González-Morena J.M., Sánchez-Gómez F.J., Vida Y., Pérez-Inestrosa E., Salas M., Montañez M., Altomare A., Aldini G, Pajares M.A., Pérez-Sala D. Amoxicillin Haptenation of α-Enolase is Modulated by Active Site Occupancy and Acetylation. Front Pharmacol. 2022 Jan 13:12:807742. doi: 10.3389/fphar.2021.807742.
• Garzon D., Ariza A., Regazzoni L., Clerici R., Altomare A., Sirtori F.R., Carini M., Torres M.J., Perez-Sala D., Aldini G. Mass spectrometric strategies for the identification and characterization of human serum albumin covalently adducted by amoxicillin: ex vivo studies. Chem Res Toxicol. 2014 Sep 15;27(9):1566-74. doi: 10.1021/tx500210e.