Conformational Studies of Tachykinin Peptides Using NMR Spectroscopy

A conformational analysis in water and DMSO of two tachykinin family peptides (scyliorhinin I (ScyI) and scyliorhinin II (ScyII)) was carried out by 1D and 2D NMR (DQF-COSY, TOCSY, HMQC, HMBC, NOESY and ROESY) and molecular dynamics calculation methods. In DMSO, two groups of conformations (major and minor) were obtained for both peptides based on the experimental data. The conformations proposed for ScyI represent a folded structure, which shows certain similarities to the structures reported for other NK-1 and NK-2 tachykinin agonists. In water ScyII displays a flexible, extended structure, whereas in DMSO the structure is more compact and, in the fragment from the centre to the C-terminus, several -turns may be present.     

Conformational Studies of Tachykinin Peptides Using NMR Spectroscopy

Summary A conformational analysis in water and DMSO of two tachykinin family peptides (scyliorhinin I (ScyI) and scyliorhinin II (ScyII)) was carried out by 1D and 2D NMR (DQF-COSY, TOCSY, HMQC, HMBC, NOESY and ROESY) and molecular dynamics calculation methods. In DMSO, two groups of conformations (major and minor) were obtained for both peptides based on the experimental data. The conformations proposed for ScyI represent a folded structure, which shows certain similarities to the structures reported for other NK-1 and NK-2 tachykinin agonists. In water ScyII displays a flexible, extended structure, whereas in DMSO the structure is more compact and, in the fragment from the centre to the C-terminus, several β-turns may be present.