The free-energy surface (FES) of protein-ligand binding contains information useful for drug design. Here we show how to exploit a free-energy minimum of a protein-ligand complex identified by metadynamics simulations to design a new EphA2 antagonist with improved inhibitory potency.
Exploiting Free-Energy Minima to Design Novel EphA2 Protein-Protein Antagonists: From Simulation to Experiment and Return / Russo, Simonetta; Callegari, Donatella; Incerti, Matteo; Pala, Daniele; Giorgio, Carmine; Brunetti, Jlenia; Bracci, Luisa; Vicini, Paola; Barocelli, Elisabetta; Capoferri, Luigi; Rivara, Silvia; Tognolini, Massimiliano; Mor, Marco; Lodola, Alessio. - In: CHEMISTRY-A EUROPEAN JOURNAL. - ISSN 0947-6539. - 22:24(2016), pp. 8048-8052. [10.1002/chem.201600993]
Exploiting Free-Energy Minima to Design Novel EphA2 Protein-Protein Antagonists: From Simulation to Experiment and Return
RUSSO, Simonetta;CALLEGARI, DONATELLA;INCERTI, Matteo;PALA, Daniele;GIORGIO, Carmine;VICINI, Paola;BAROCELLI, Elisabetta;CAPOFERRI, LUIGI;RIVARA, Silvia;TOGNOLINI, Massimiliano;MOR, Marco;LODOLA, Alessio
2016-01-01
Abstract
The free-energy surface (FES) of protein-ligand binding contains information useful for drug design. Here we show how to exploit a free-energy minimum of a protein-ligand complex identified by metadynamics simulations to design a new EphA2 antagonist with improved inhibitory potency.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
