Protein-drug conjugates utilize cytotoxic organic compounds that are either covalently linked to carrier proteins or interact with them through non-covalent forces. In this study, we demonstrate that solid-state NMR can effectively detect ligand-induced effects, which can be directly associated with structural and dynamic changes influencing the stability of macromolecular complexes.
SOLID-STATE NMR TO DESIGN CHALLENGING PROTEIN-DRUG CONJUGATES / Linda Cerofolini, Kristian Vasa, Elisa Bianconi, Maria Salobehaj, Giulia Cappelli, Alice Bonciani, Giulia Licciardi, Anna Pérez-Ràfols, Luis David Padilla Cortés, Sabrina Antonacci, Domenico Rizzo, Enrico Ravera, Caterina Viglianisi, Vito Calderone, Giacomo Parigi, Claudio Luchinat, Antonio Macchiarulo, Stefano Menichetti, Marco Fragai. - ELETTRONICO. - (2024), pp. 17-17. (Intervento presentato al convegno 51st National Congress on Magnetic Resonance).
SOLID-STATE NMR TO DESIGN CHALLENGING PROTEIN-DRUG CONJUGATES
Linda Cerofolini;Kristian Vasa;Maria Salobehaj;Giulia Cappelli;Alice Bonciani;Giulia Licciardi;Anna Pérez-Ràfols;Sabrina Antonacci;Domenico Rizzo;Enrico Ravera;Caterina Viglianisi;Vito Calderone;Giacomo Parigi;Claudio Luchinat;Stefano Menichetti;Marco Fragai
2024
Abstract
Protein-drug conjugates utilize cytotoxic organic compounds that are either covalently linked to carrier proteins or interact with them through non-covalent forces. In this study, we demonstrate that solid-state NMR can effectively detect ligand-induced effects, which can be directly associated with structural and dynamic changes influencing the stability of macromolecular complexes.
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