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• W2078397865 abstract "Ligand binding to neuropeptide Y (NPY) receptors Y1, Y2, Y4, and Y5 from guinea-pig was investigated using the two NPY-galanin hybrids M32 (galanin1-13-NPY25-36-amide) and M242 ([D-Trp(32)]M32). The affinity of M32 for Y1, Y2, and Y4 receptors was 13, 4, and 30nM, respectively, similar to that of NPY18-36 and NPY22-36 but 40-fold to 300-fold lower than the affinity of intact porcine NPY. M242 bound to the Y1, Y2, and Y4 receptors with 9-fold to 20-fold lower affinity than did M32. The affinities of M32 and M242 for Y5 were 400 and 800 nM, respectively. Thus, M32 seems to gain affinity relative to both of its constituent peptide portions although the NPY25-36 part may be sufficient for NPY-receptor recognition, especially at the Y2 receptor. This suggests that the galanin portion of M32 influences and/or stabilizes the conformation of the NPY portion, similar to the effect seen for the NPY portion of M32 in binding to galanin receptors." @default.
• W2078397865 created "2016-06-24" @default.
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• W2078397865 date "2001-06-01" @default.
• W2078397865 modified "2023-09-23" @default.
• W2078397865 title "Binding of chimeric npy/galanin peptides M32 and M242 to cloned neuropeptide Y receptor subtypes Y1, Y2, Y4, and Y5" @default.
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• W2078397865 doi "https://doi.org/10.1054/npep.2001.0856" @default.
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