Conformational properties of deltorphin: New features of the δ‐opioid receptor

FEBS Letters

Balboni, G.³  Marastoni, M.³  Salvadori, S.³  Temussi, P.A.²  Tancredi, T.¹  Picone, D.²  Tomatis, R.³ 

[1] ICMIB del CNR, Arco Felice, Napoli Italy;Dipartimento di Chimica, University of Naples, via Mezzocannone 4, 80134 Napoli, Italy;Dipartimento di Scienze Farmaceutiche, University of Ferrara, via Scandiana 21, Ferrara, Italy

关键词: Opioid;    Selectivity;    Deltorphin;    Dermorphin;    NMR;    Conformation;    DADLE;    [D-Ala2;    D-Leu5]enkephalin;    DPDPE;    [D-Pen2;    D-Pen5]enkephalin;    DAGO;    Tyr-D-Ala-Gly-MePhe-NHCH2-CH2OH;    MVD;    mouse Vas Deferens;    GPI;    guinea pig ileum;    DMSOd6;    perdeuterated dimethylsulfoxide;    D2O;    deuterium oxide;    DQF-COSY;    double-quantum filtered correlation spectroscopy;    HOHAHA;    homonuclear Hartman-Hahn spectroscopy;    1D;    one dimensional;    2D;    two dimensional;    NOESY;    nuclear Overhauser effect spectroscopy;    NMR;    nuclear magnetic resonance. Standard three letter codes are used for amino acid residue identification;   

DOI  :  10.1016/0014-5793(89)81353-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Deltorphin is an opioid peptide with the sequence H-Tyr-D-Met-Phe-His-Leu-Met-Asp-NH₂, 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-NH₂), a μ selective peptide isolated from the same natural source, prompted a comparative conformational study. A ¹H-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.

【 授权许可】

Unknown