Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin

Abstract

The usefulness of 2,2,2-trifluoroethanol titration as a means of distinguishing between intramolecular peptide-peptide hydrogen bonding on the one hand and intermolecular peptide-peptide and peptide-solvent hydrogen bonding on the other has been investigated with neurohypophyseal hormones, and the results have been compared with those of other methods. The chemical shifts (220 MHz) of the resonances of amide NH and aromatic CH protons of oxytocin, lysine vasopressin, deamino-lysine vasopressin, and deamino-8-tosyllysine vasopressin were monitored as the solvent composition was progressively varied from 100% dimethylsulfoxide to 100% 2,2,2-trifluoroethanol. The overall backbone conformation of oxytocin appears to be retained, and possibly somewhat stabilized, during the solvent transition, while the backbone, particularly the acyclic component, of lysine vasopressin and its analogs is subject to solvent-induced perturbation.