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Conformational Analysis by NMR and Distance-Geometry Techniques of Deltorphin Analogs

✍ Scribed by Ettore Benedetti; Carla Isernia; Flavia Nastri; Carlo Pedone; Michele Saviano; Dale F. Mierke; Pietro Melchiorri; Lucia Negri; Rosa Luisa Potenza; Cinzia Severini; Vittorio Erspamer

Publisher: John Wiley and Sons
Year: 1998
Tongue: English
Weight: 353 KB
Volume: 1998
Category: Article
ISSN: 1434-193X
DOI: 10.1002/(sici)1099-0690(199811)1998:11<2279::aid-ejoc2279>3.0.co;2-0

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✦ Synopsis

To identify the peptide conformation that is preferentially secondary structural elements. The analysis of the average properties of these compounds indicate the presence of some recognized by the receptor, we have synthetized by solidphase method a series of deltorphin I analogs with increasing distinct conformational preferences that can be related to the observed opioid receptor selectivities. Selectivity for the δselectivity for δand µ-opioid receptor. Structure-selectivity relationship of these peptides were evaluated on the basis and µ-opioid receptors can be ascribed to the spatial arrangement of the aromatic moieties. In addition, of receptor-binding properties and conformational features, computed by two-dimensional NMR spectra and distance-substitutions in position 2 and 4 are important for the correct arrangement and must be taken into account in the design geometry techniques. These compounds in solution are present with a large number of conformers with no defined of δ-opioid receptor-selective ligands.

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