Exploring the conformational space of the μ-opioid agonists endomorphin-1 and endomorphin-2

Balázs Leitgeb, A. Szekeres

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Endomorphins (EM1, H-Tyr-Pro-Trp-Phe-NH2 and EM2, H-Tyr-Pro-Phe-Phe-NH2) were isolated from bovine brain, and these flexible tetrapeptides are highly potent and selective ligands for the μ-opioid receptor. We have explored the Φ22 and Φ21 conformational spaces of all four types of EMs (neutral or charged N-terminal amino groups, cis or trans Tyr 1-Pro2 peptide bonds) using the simulated annealing. The conformational distributions were illustrated in the three-dimensional Ramachandran plots and three-dimensional pseudo-Ramachandran plots, and the mainly populated Φ22 and Φ 21 regions were determined. The main combinations of side-chain rotamers of the Tyr1, Trp3 and Phe 4 residues for EM1 and the Tyr1, Phe3 and Phe4 residues for EM2 were identified in χ1 conformational space.

Original languageEnglish
Pages (from-to)337-344
Number of pages8
JournalJournal of Molecular Structure: THEOCHEM
Volume666-667
DOIs
Publication statusPublished - Dec 29 2003

Fingerprint

Opioid Receptors
Simulated annealing
Opioid Analgesics
Peptides
Brain
plots
Ligands
simulated annealing
peptides
brain
ligands
endomorphin 2
endomorphin 1

Keywords

  • Endomorphin-1
  • Endomorphin-2
  • Simulated annealing
  • Three-dimensional pseudo-Ramachandran plot
  • Three-dimensional Ramachandran plot

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Computational Theory and Mathematics
  • Atomic and Molecular Physics, and Optics

Cite this

Exploring the conformational space of the μ-opioid agonists endomorphin-1 and endomorphin-2. / Leitgeb, Balázs; Szekeres, A.

In: Journal of Molecular Structure: THEOCHEM, Vol. 666-667, 29.12.2003, p. 337-344.

Research output: Contribution to journalArticle

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N2 - Endomorphins (EM1, H-Tyr-Pro-Trp-Phe-NH2 and EM2, H-Tyr-Pro-Phe-Phe-NH2) were isolated from bovine brain, and these flexible tetrapeptides are highly potent and selective ligands for the μ-opioid receptor. We have explored the Φ2-Ψ2 and Φ2-Ψ1 conformational spaces of all four types of EMs (neutral or charged N-terminal amino groups, cis or trans Tyr 1-Pro2 peptide bonds) using the simulated annealing. The conformational distributions were illustrated in the three-dimensional Ramachandran plots and three-dimensional pseudo-Ramachandran plots, and the mainly populated Φ2-Ψ2 and Φ 2-Ψ1 regions were determined. The main combinations of side-chain rotamers of the Tyr1, Trp3 and Phe 4 residues for EM1 and the Tyr1, Phe3 and Phe4 residues for EM2 were identified in χ1 conformational space.

AB - Endomorphins (EM1, H-Tyr-Pro-Trp-Phe-NH2 and EM2, H-Tyr-Pro-Phe-Phe-NH2) were isolated from bovine brain, and these flexible tetrapeptides are highly potent and selective ligands for the μ-opioid receptor. We have explored the Φ2-Ψ2 and Φ2-Ψ1 conformational spaces of all four types of EMs (neutral or charged N-terminal amino groups, cis or trans Tyr 1-Pro2 peptide bonds) using the simulated annealing. The conformational distributions were illustrated in the three-dimensional Ramachandran plots and three-dimensional pseudo-Ramachandran plots, and the mainly populated Φ2-Ψ2 and Φ 2-Ψ1 regions were determined. The main combinations of side-chain rotamers of the Tyr1, Trp3 and Phe 4 residues for EM1 and the Tyr1, Phe3 and Phe4 residues for EM2 were identified in χ1 conformational space.

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