Biotin Ergopeptide Probes for Dopamine Receptors

Marc Vendrell, Anabel Molero, Sergio Gonzalez, Kamil Perez-Capote, Carme Lluis, Peter J. McCormick, Rafael Franco, Antoni Cortes, Vicent Casado, Fernando Albericio, Miriam Royo*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The incorporation of chemical modifications into the structure of bioactive compounds is often difficult because the biological properties of the new molecules must be retained with respect to the native ligand. Ergopeptides, with their high affinities at D(1) and D(2) dopamine receptors, are particularly complex examples. Here, we report the systematic derivatization of two ergopeptides with different peptide-based spacers and their evaluation by radioligand binding assays. Selected spacer-containing ergopeptides with minimal biological alteration and a proper anchoring point were further derivatized with a biotin reporter. Detailed characterization studies identified 13 as a biotin ergopeptide maintaining high affinity and agonist behavior at dopamine receptors, being a useful tool for the study of heteromers involving D(1)R, D(2)R, or D(3)R.

Original languageEnglish
Pages (from-to)1080-1090
Number of pages11
JournalJournal of Medicinal Chemistry
Volume54
Issue number4
DOIs
Publication statusPublished - 24 Feb 2011

Keywords

  • SOLID-PHASE SYNTHESIS
  • CHEMICAL GENETICS
  • HISTAMINE H-3
  • LIVING CELLS
  • ADENOSINE
  • AGONISTS
  • BINDING
  • HETEROOLIGOMERS
  • ANTAGONISTS
  • CHEMISTRY

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