Molecular mechanism of interactions between inhibitory tripeptide GEF and angiotensin-converting enzyme in aqueous solutions by molecular dynamic simulations

Abstract A novel ACE-inhibitory tripeptide Gly-Glu-Phe (GEF) was used to study the molecular mechanism of interactions with ACE. Molecular docking and molecular dynamics simulations were performed to investigate the interactions between GEF and ACE of different domain (C-domain and N-domain) in the aqueous solutions. RMSD , SASA , RMSF , binding energy and hydrogen bonding were analyzed to reveal the molecular mechanism between ligand and acceptor in a micro level.