Secondary Structure of the Cyclic Moiety of the Peptide Hormone Oxytocin and Its Deamino Analog

Abstract

The secondary structure of the cyclic moiety of oxytocin and deamino-oxytocin has been determined by nuclear magnetic resonance spectroscopy (220 MHz). Oxytocin, in a dimethylsulfoxide-methanol mixture, contains a beta-turn involving the sequence -L-tyrosyl-L-isoleucyl-L-glutaminyl-L-asparaginyl-. Deamino-oxytocin, in addition to the beta-turn, contains a hydrogen bond involving the amide hydrogen of the tyrosine residue and the peptide carbonyl group of the asparagine residue, resulting in an antiparallel beta-type conformation for the ring component. An initial attempt has been made to relate conformational features of the hormonal peptides to their biological activity.