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Conformation of a diastereoisomeric pair of enkephalin analogues: A 400 MHz 1 H NMR study
Author(s) -
Bajusz S.,
Casy A. F.
Publication year - 1984
Publication title -
organic magnetic resonance
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0030-4921
DOI - 10.1002/mrc.1270220610
Subject(s) - dipeptide , chemistry , enkephalin , intramolecular force , stereochemistry , hydrogen bond , peptide , receptor , molecule , organic chemistry , biochemistry , opioid
1 H NMR spectra recorded at 400 MHz of the enkephalin analogues Tyr‐ D ‐NIe‐Gly‐Phe‐ D (and L )‐NIeS and the dipeptide Ac‐Phe‐ D ‐NIeS as solutes in DMSO‐d 6 are reported and assigned. A preferred conformation of the D 2 L 5 peptide is proposed, based on evidence of an intramolecular hydrogen bond between Phe 4 NH and Tyr 1 CO and NH/ a ‐CH coupling constants. The possibility of conformational differences between the isomeric peptides accounting for differences in their ability to bind to δ‐opiate receptors is discussed.