Influence of polar side chains modifications on the dual enkephalinase inhibitory activity and conformation of human opiorphin, a pain perception related peptide

Mònica Rosa, Filipa Marcelo, Luis P. Calle, Catherine Rougeot, Jesús Jiménez-Barbero, Gemma Arsequell, Gregorio Valencia

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

The dual inhibitory action of the pain related peptide opiorphin (H-Gln-Arg-Phe-Ser-Arg-OH) against neutral endopeptidase (NEP) and aminopeptidase N (AP-N) was further investigated by a SAR study involving minor modifications on the polar side chains of Arg residues and glycosylation with monosaccharides at Ser. None of them exerted dual or individual inhibitory potency superior than opiorphin. However, the correlations deduced offer further proof for the key role of these residues upon the binding and bioactive conformational stabilization of opiorphin. NMR conformational studies on the glycopeptides suggest that they are still very flexible compounds that may attain their respective bioactive conformations.

Original languageEnglish
Pages (from-to)5190-5193
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume25
Issue number22
DOIs
Publication statusPublished - 15 Nov 2015

Keywords

  • AP-N
  • Glycopeptides pain
  • Neutral endopeptidase
  • Opiorphin analogs
  • SAR study

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