Ki: 25.7 nM for Y1

Neuropeptide Y (NPY), a 36-residue peptide amide isolated originally from porcine brain, is a member of homologous hormone family including peptide YY (PYY) and pancreatic polypeptide (PP). It is the most abundant peptide in the mammalian brain and has been shown to exhibit a wide spectrum of central and peripheral activities. These actions are mediated by at least six G-protein coupled receptor subtypes denoted as Y1, Y2, Y3, Y4, Y5, and y6. BVD 10 is a highly selective and potent neuropeptide Y (NPY) Y1 receptor antagonists.

In vitro: The inability to form such hydrogen bonding in BVD 10 may prevent or perturb the C-terminus reverse turn, which may contribute, at least in part, to the increased Y1 selectivity [1]. Moreover, BVD 10 and its NPY analogue peptide BVD15 were characterized conformationally. The two peptides exhibit different secondary structure characteristics in trifluoroethanol. Molecular modeling studies suggested that the C-terminus Tyr9 is oriented in different directions in the two peptides. The difference in the structures observed may contribute to the Y1 selectivity of BVD 10 relative to BVD 15 [2].

In vivo: No animal in vivo data have been reported so far.

Clinical trial: Up to now, BVD 10 is still in the preclinical development stage.