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Structure–Activity relationship of tetrapeptides related to dermorphin: A 500-MHz 1H-nmr study

✍ Scribed by M. A. Castiglione-Morelli; T. Tancredi; E. Trivellone; G. Balboni; M. Marastoni; S. Salvadori; R. Tomatis; P. A. Temussi

Publisher
Wiley (John Wiley & Sons)
Year
1988
Tongue
English
Weight
551 KB
Volume
27
Category
Article
ISSN
0006-3525

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✦ Synopsis

Several tetrapeptide analogs of dermorphin have been studied by means of 'H-nmr spectroscopy at 500 MHz in DMSO-d,. 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 p 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.

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