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- W1998197178 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 D1 and D2 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 D1R, D2R, or D3R." @default.
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- W1998197178 date "2011-01-31" @default.
- W1998197178 modified "2023-10-06" @default.
- W1998197178 title "Biotin Ergopeptide Probes for Dopamine Receptors" @default.
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- W1998197178 doi "https://doi.org/10.1021/jm101566d" @default.
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