Structure-activity relatioships of tetrapeptides related to dermorphin: a 500-MHz 1H-nmr study
BALBONI, GIANFRANCO;
1988-01-01
Abstract
Several tetrapeptide analogs of dermorphin have been studied by means of 1H-nmr spectroscopy at 500 MHz in DMSO-d6. In spite of the unfavorable properties of the solvent, it is possible to extract key structural information that, combined with the biological activity of the peptides, yields a structure–activity relationship that is consistent with our model of the μ receptor site. In particular, the importance of the orientation of the aromatic ring of the third residue, hypothesized in the theoretical model, is now substantiated. The shape of the P subsite of the receptor is also indirectly defined by the shape of several bulky side chains of the third residue.Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.