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2000
Volume 4, Issue 1
  • ISSN: 1568-0266
  • E-ISSN: 1873-4294

Abstract

Despite of the recent advances in the structural investigation of complex molecules, the comprehension of the 3D features responsible for the interaction between opioid peptides and μ- opioid receptors still remains an elusive task. This has to be attributed to the intrinsic nature of opioid peptides, which can assume a number of different conformations of similar energy, and to the flexibility of the receptorial cavity, which can modify its inner shape to host different ligands. Due to this inherent mobility of the ligand-receptor system, massive efforts devoted to the definition of a rigid bioactive conformation to be used as a template for the design of new pharmacologically active compounds might be overstressed. The future goal might be the design of peptide or nonpeptide ligands capable of maximizing specific hydrophobic interactions. This review covers the recent opinions emerged on the nature of the ligand-receptor interaction, and the development of suitable models for the determination of the bioactive conformation of peptide ligands active towards m-opioid receptors.

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/content/journals/ctmc/10.2174/1568026043451627
2004-01-01
2025-05-05
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  • Article Type:
    Review Article
Keyword(s): antinociception; bioactive conformation; endomorphins; Opioid peptides
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