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;
2016-01-01
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.
File in questo prodotto:
| File | Dimensione | Formato | |
|---|---|---|---|
|
Exploiting Free-Energy Minima.pdf
non disponibili
Descrizione: Articolo
Tipologia:
PDF editoriale
Licenza:
NON PUBBLICO - Accesso privato/ristretto
Dimensione
1.98 MB
Formato
Adobe PDF
|
1.98 MB | Adobe PDF | Visualizza/Apri Richiedi una copia |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
Utilizza questo identificativo per citare o creare un link a questo documento:
https://hdl.handle.net/11365/1007133