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Structure–Activity relationship of tetrapeptides related to dermorphin: A 500‐MHz 1 H‐nmr study
Author(s) -
CastiglioneMorelli M. A.,
Tancredi T.,
Trivellone E.,
Balboni G.,
Marastoni M.,
Salvadori S.,
Tomatis R.,
Temussi P. A.
Publication year - 1988
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360270903
Subject(s) - dermorphin , tetrapeptide , chemistry , stereochemistry , residue (chemistry) , nuclear magnetic resonance spectroscopy , side chain , two dimensional nuclear magnetic resonance spectroscopy , peptide , receptor , biochemistry , organic chemistry , opioid peptide , opioid , polymer
Several tetrapeptide analogs of dermorphin have been studied by means of 1 H‐nmr spectroscopy at 500 MHz in DMSO‐d 6 . 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.

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