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EnglishSeveral 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.
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| Titolo: | Structure-activity relatioships of tetrapeptides related to dermorphin: a 500-MHz 1H-nmr study |
| Autori: | |
| Data di pubblicazione: | 1988 |
| Rivista: | |
| 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. |
| Handle: | http://hdl.handle.net/11584/6633 |
| Tipologia: | 1.1 Articolo in rivista |
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