Molecular dynamics simulations and 2D-NOESY spectroscopy studied on conformational features of ACE-inhibitory tripeptide Gly-Glu-Phe in aqueous and DMSO solutions

Molecular dynamics simulations revealed that the ACE inhibitor tripeptide GEF is more flexible in aqueous solution than that in DMSO solution. The conformations of GEF can quickly convert from extended states to folded states in aqueous solution, but the extended state is hardly observed in DMSO solution. Furthermore, the GEF prefers more extended state than that in DMSO solution, which is confirmed by 2D-NOESY spectrum.