Exploiting Free‐Energy Minima to Design Novel EphA2 Protein–Protein Antagonists: From Simulation to Experiment and Return | Zendy

Russo Simonetta | Zendy; Callegari Donatella | Zendy; Incerti Matteo | Zendy; Pala Daniele | Zendy; Giorgio Carmine | Zendy; Brunetti Jlenia | Zendy; Bracci Luisa | Zendy; Vicini Paola | Zendy; Barocelli Elisabetta | Zendy; Capoferri Luigi | Zendy; Rivara Silvia | Zendy; Tognolini Massimiliano | Zendy; Mor Marco | Zendy; Lodola Alessio | Zendy

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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.

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