Premium
Structure–activity relationships of neuropeptide Y analogues with respect to Y 1 and Y 2 receptors
Author(s) -
BeckSickinger Annette G.,
Jung Günther
Publication year - 1995
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360370207
Subject(s) - chemistry , receptor , affinities , neuropeptide y receptor , binding affinities , neuropeptide , stereochemistry , alanine , amino acid , biochemistry
Secondary structure investigations, affinities, and activities of neuropeptide Y analogues with respect to the Y 1 and the Y 2 receptor are reviewed. The results are discussed with respect to the different prerequisites for affinities to both receptor subtypes. The results from a systematic scanning of the hormone using L ‐alanine and from a large variety of discontinuous and cyclic analogs suggest that two different conformations of neuropeptide Y are adopted at the Y 1 and Y 2 receptors. Whereas a C‐terminal turn structure is suggested for Y 1 receptor affinity, an α‐helical conformation of the C‐terminus is afforded for good binding to the Y 2 receptor. © 1994 John Wiley & Sons, Inc.