Biotin ergopeptide probes for dopamine receptors

Vendrell, Marc, Molero, Anabel, González, Sergio, Pérez-Capote, Kamil, Lluis, Carme, McCormick, Peter J., Franco, Rafael, Cortés, Antoni, Casadó, Vicent, Albericio, Fernando and Royo, Miriam (2011) Biotin ergopeptide probes for dopamine receptors. Journal of Medicinal Chemistry, 54 (4). pp. 1080-1090. ISSN 0022-2623

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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 and D 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 R, D R, or D R.

Item Type: Article
Faculty \ School: Faculty of Science > School of Pharmacy
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Depositing User: Pure Connector
Date Deposited: 13 Jan 2014 13:26
Last Modified: 24 Oct 2022 05:56
DOI: 10.1021/jm101566d

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