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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 ; Reiser, Oliver



Abstract

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 (beta Cbu) or (1R,2S)cyclopentane (beta 6Cpe) fl-amino acids, which display exclusively Y4R affinity. In particular, [beta ...

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