Collision-induced liquid secondary-ion mass spectra of oxytocin derivatives. A study of the influence of modifications in the disulfide bond on the adjacent peptide bond cleavage.

The influence of the inductive effect of modifications in the disulfide bridge in oxytocin analogs on the cleavage of the neighboring peptidic bond was studied. A correlation between the inductive constant of the group in the disulfide bridge and the particular fragment ion abundance was observed.