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2012 | 10 | 1 | 172-179
Article title

Structural comparison of endomorphin-2 and its conformationally restricted analog

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In the present study, the effect of a conformational constraint introduced into the endomorphin-2 (Tyr-Pro-Phe-Phe-NH2, EM-2) structure was studied using computational analysis and radioligand binding assay. EM-2 was modified by connecting nitrogen atoms of both phenylalanine residues by a methylene bridge. The obtained analog did not bind to the µ- or δ-opioid receptors in the in vitro studies. The computational analysis of this analog showed twisted, type IV turns and the absence of canonical β-turns typical for the EM-2 structure, which can be explained by the lack of hydrogen bonds involving Phe4. Our results show that the introduction of chemical constraint in the EM-2 structure has a significant effect on opioid receptor affinity and in vitro bioactivity.
Physical description
1 - 2 - 2012
24 - 11 - 2011
  • Biological Research Center of the Hungarian Academy of Sciences
  • Medical University
  • Medical University
  • Gdansk University
  • Biological Research Center of the Hungarian Academy of Sciences
  • Medical University
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