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Exploiting Free‐Energy Minima to Design Novel EphA2 Protein–Protein Antagonists: From Simulation to Experiment and Return
Author(s) -
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
Publication year - 2016
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201600993
Subject(s) - metadynamics , maxima and minima , ligand (biochemistry) , energy (signal processing) , chemistry , computer science , physics , molecular dynamics , computational chemistry , biochemistry , receptor , mathematics , mathematical analysis , quantum mechanics
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.