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Conformational properties of deltorphin: New features of the δ‐opioid receptor
Author(s) -
Temussi P.A.,
Picone D.,
Tancredi T.,
Tomatis R.,
Salvadori S.,
Marastoni M.,
Balboni G.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81353-5
Subject(s) - dermorphin , opioid peptide , chemistry , receptor , peptide , stereochemistry , opioid receptor , selectivity , opioid , peptide sequence , sequence (biology) , biochemistry , gene , catalysis
Deltorphin is an opioid peptide with the sequence H‐Tyr‐D‐Met‐Phe‐His‐Leu‐Met‐Asp‐NH 2 , recently isolated from the skin of Phyllomedusa sauvagei . Its enormous selectivity towards the δ‐opioid receptor and the similarity of the N‐terminal part of the sequence with that of dermorphin (H‐Tyr‐D‐Ala‐Phe‐Gly‐Tyr‐Pro‐Ser‐NH 2 ), a μ selective peptide isolated from the same natural source, prompted a comparative conformational study. A 1 H‐NMR study in two different solvent systems showed that the conformational preferences of the N‐terminal sequences of the two peptides are similar. The different selectivities towards opioid receptors have been interpreted in terms of charge effects. Besides a general trend consistent with the role of the membrane in the preselection of the peptides, the present study demonstrates the crucial role played by charged residues in the interaction inside the receptors.