Examination of the conformational meaning of "δ-address" in the dermenkephalin sequence

Gregory V. Nikiforovich, Victor J. Hruby

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47 Scopus citations


Comprehensive energy calculations were applied to four opioid-related peptides with different receptor selectivities, namely the δ-selective dermenkephalin (Tyr-D-Met-Phe-His-Leu-Met-Asp-NH2, DRE), the μ-selective dermorphin (Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2, DRM) and their "hybrid" peptides DRM/DRE (Tyr-D-Ala-Phe-Gly-Leu-Met-Asp-NH2) and DRE/DRM (Tyr-D-Met-Phe-His-Tyr-Pro-Ser-NH2). It was shown that the N-terminal tripeptide "μ-messages" in the δ-selective ligands DRE and DRM/DRE can possess similar low energy space arrangements of their functionally important elements (the N-terminal α-amino group and the aromatic moieties of Tyr and Phe), but that these are different from the space arrangement of these moieties in μ-selective DRM and DRE/DRM. These results suggest that the C-terminal tripeptide "δ-address" in DRE may influence the conformation of the "μ-message" in DRM. A refined model for the δ-receptor-bound conformation of DRE is proposed based on these calculations which is similar to that previously suggested for the cyclic δ-selective peptide [D-Pen2, D-Pen5]enkephalin (DPDPE). This model also has partial correspondence with the structure of the δ-selective alkaloid naltrindole.

Original languageEnglish (US)
Pages (from-to)521-527
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Dec 14 1990

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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