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Updated: Aug 19, 2026

Characterization of G Protein-coupled Receptors by a Fluorescence-based Calcium Mobilization Assay
Published on: July 28, 2014
Cyclopeptide analogs for characterization of the neuropeptide Y Y2-receptor
A G Beck-Sickinger1, H Köppen, E Hoffmann
1Institute of Organic Chemistry, University of Tübingen, Germany.
Abstract:
A discontinuous 17-amino acid peptide analog of neuropeptide Y (NPY), NPY 1-4-Ahx-25-36 containing 6-aminohexanoic acid instead of the residues 5 to 24, was found to bind preferentially to Y2 subtypes of NPY receptors. In order to further characterize the binding site, three different types of cyclic analogs were synthesized. Firstly lactamisation between residues 2 and 30 led to the most selective Y2-agonist, secondly lactamisation between the N-terminus and residue 31 reduced binding significantly. Thirdly, any cyclization including the C-terminus led to an inactive compound. Circular dichroism revealed different conformations for the three analogs with reduced alpha-helical content in comparison to the linear ana-log. The different conformation of the peptides has been confirmed by molecular dynamics simulations. A model for peptide-receptor interaction is suggested.
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