Exploiting Free‐Energy Minima to Design Novel EphA2 Protein–Protein Antagonists: From Simulation to Experiment and Return. Issue 24 (3rd May 2016)

• Record Type: Journal Article
• Authors: 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
• Is Part Of: Chemistry. Volume 22:Issue 24(2016)
• Page Start: 8048
• Page End: 8052
• Publication Date: 2016-05-03
• Subjects: computational chemistry -- drug design -- metadynamics -- steroids -- surface plasmon resonance; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201600993
• Languages: English
• ISSNs: 0947-6539

Abstract

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. Abstract : The free‐energy surface (FES) of protein–ligand binding contains information useful for drug design. A free‐energy minimum of a protein–ligand complex identified by metadynamics simulations can be exploited to design a new EphA2 antagonist with improved inhibitory potency.