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

@article{Temussi1989ConformationalPO,
  title={Conformational properties of deltorphin: New features of the $\delta$‐opioid receptor},
  author={Pierandrea Temussi and Delia Picone and Teodorico Tancredi and Roberto Tomatis and Severo Salvadori and Mauro Marastoni and Gianfranco Balboni},
  journal={FEBS Letters},
  year={1989},
  volume={247}
}

New insights on μ/δ selectivity of opioid peptides: Conformational analysis of deltorphin analogues

TLDR
Deltorphins, in fact, are three heptapeptides characterized by a message domain typical of μ‐selective peptides, but endowed of an extremely high δ selectivity, the highest of all natural opioid peptides.

Quantitative two‐dimensional nmr study of dermenkephalin, a highly potent and selective δ‐opioid peptide

TLDR
The overall data should provide realistic starting models for energy minimization and modelization studies, and the nonuniform values of the temperature coefficient may reflect an equilibrium mixture of folded and extended conformers.

Comparative conformational analyses of μ‐selective dermorphin and §‐selective deltorphin‐II in aqueous solution by 1H‐NMR spectroscopy

TLDR
Two-dimensional 1H-NMR methods have been used to obtain complete proton resonance assignments and possible solution conformations of dermorphin and deltorphin-II, naturally occurring mu- and delta-selective opioids, respectively, in order to examine the conformational characteristics that are closely related to the selectivities towards mu/delta-opioid receptors.

Folded conformations of the delta-selective opioid dermenkephalin with head-to-tail interactions. A simulated annealing study through NMR restraints.

TLDR
To examine the conformational characteristics that are related to the selectivity of dermenkephalin towards the delta-receptor, 50 NOE restraints, 7 dihedral angles, and 20 resulting conformers with no severe distance restraint violation were used in simulated annealing and energy minimization procedures.

Asymmetric Synthesis and Conformational Analysis by NMR Spectroscopy and MD of Aba‐ and α‐MeAba‐Containing Dermorphin Analogues

Dermorphin analogues, containing a (S)‐ and (R)‐4‐amino‐1,2,4,5‐tetrahydro‐2‐benzazepin‐3‐one scaffold (Aba) and the α‐methylated analogues as conformationally constrained phenylalanines, were

Opioid activity of dermenkephalin analogues in the guinea‐pig myenteric plexus and the hamster vas deferens

TLDR
The results obtained emphasise the importance of a negative charge at the C‐terminus of dermenkephalin for selectivity at the δ‐opioid receptor and the role that the d‐configuration plays in determining the bioactive folding of these highly active peptides.

Opioid receptor selectivity reversal in deltorphin tetrapeptide analogues.

Investigation of the structural parameters involved in the delta-opioid selectivity of several families of opioid peptides.

TLDR
Direct comparison between the biochemical profiles of the [pClPhe4] analogs of the linear constrained peptides and their parent compounds shows that the addition of an electronegative atom on the Phe4 residue of enkephalin sequences is not an absolute parameter for delta-selectivity improvement.

Solution conformations of deltorphin-I obtained from combined use of quantitative 2D-NMR and energy calculations: a comparison with dermenkephalin.

TLDR
Results suggest that conformational attributes that are common to dermenkephalin and deltorphin-I, i.e., the backbone conformation of the N-terminal tetrapeptide and preferential orientations in the side-chain of Tyr1 (t) and Phe3 (g-) underlie their ability to bind with high selectivity to the delta-opioid receptor.

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    Proceedings of the National Academy of Sciences of the United States of America
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