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.

Russo, S., Callegari, D., Incerti, M., Pala, D., Giorgio, C., Brunetti, J., et al. (2016). Exploiting Free-Energy Minima to Design Novel EphA2 Protein-Protein Antagonists: From Simulation to Experiment and Return. CHEMISTRY-A EUROPEAN JOURNAL, 22(24), 8048-8052 [10.1002/chem.201600993].

Exploiting Free-Energy Minima to Design Novel EphA2 Protein-Protein Antagonists: From Simulation to Experiment and Return

BRUNETTI, JLENIA;BRACCI, LUISA;MOR, MARCO;
2016

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.
Russo, S., Callegari, D., Incerti, M., Pala, D., Giorgio, C., Brunetti, J., et al. (2016). Exploiting Free-Energy Minima to Design Novel EphA2 Protein-Protein Antagonists: From Simulation to Experiment and Return. CHEMISTRY-A EUROPEAN JOURNAL, 22(24), 8048-8052 [10.1002/chem.201600993].
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11365/1007133