Replacement of Thr32 and Gln34 in the C-terminal neuropeptide Y fragment 25-36 by cis-cyclobutane- and cis-cyclopentane β-amino acids shifts selectivity toward the Y4 receptor

Berlicki, Lukasz, Kaske, Melanie, Gutierrez-Abad, Raquel, Bernhardt, Günther, Illa, Ona, Ortuño, Rosa, Cabrele, Chiara, Buschauer, Armin und Reiser, Oliver (2013) Replacement of Thr32 and Gln34 in the C-terminal neuropeptide Y fragment 25-36 by cis-cyclobutane- and cis-cyclopentane β-amino acids shifts selectivity toward the Y4 receptor. Journal of Medicinal Chemistry 56 (21), S. 8422-8431.

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Zusammenfassung

Neuropeptide Y (NPY) and pancreatic polypeptide (PP) control central and peripheral processes by activating the G protein coupled receptors YxR (x = 1,2,4,5). We present analogs of the C-terminal fragments 25-36 and 32-36 of NPY and PP containing (1R,2S)-cyclobutane (βCbu) or (1R,2S)-cyclopentane (βCpe), which display exclusively Y4R affinity. In particular, [βCpe34]-NPY-(25-36) is a Y4R ...

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