PMID: 7932589Oct 14, 1994Paper

Neuropeptide Y N-terminal deletion fragments: correlation between solution structure and receptor binding activity at Y1 receptors in rat brain cortex

Journal of Medicinal Chemistry
L HuM B Doughty


N alpha-Acetyl (Ac), N-terminal deletion fragments of porcine neuropeptide Y (NPY) have been synthesized and characterized for solution conformation properties by circular dichroism and for receptor binding activity at benextramine-sensitive Y1 binding sites in rat brain cortex. Sequential deletion of Tyr1, Pro2, and Ser3 had no effect on the structural (alpha-helical content of 32.5, 30.6, and 30.7%, respectively, at 1 x 10(-5) M) or aggregation (monomer to dimer transition for N alpha-Ac-NPY3-36 and N alpha-Ac-NPY4-36) properties of NPY. In contrast, deletion of Tyr1 decreased receptor binding activity in rat brain cortex by 4-fold (IC50 = 13.0 nM versus 3.75 nM for NPY), but further deletion of Pro2-Ser3 had no additional detrimental effect on receptor binding activity relative to the desTyr1 analog. Thus, Pro2 and Ser3 do not contribute either to the stability of the NPY tertiary structure nor directly to the receptor-ligand interactions. Additional removal of N-terminal amino acids Lys4-Pro5 decreased the helical content and abolished aggregation to a dimeric form of the resultant analog, results suggesting that the residues around Pro5 are important for formation of NPY's compact, pancreatic polypeptide (PP)-fold structur...Continue Reading


Sep 1, 1995·Journal of Peptide Science : an Official Publication of the European Peptide Society·B RistA G Beck-Sickinger
Feb 5, 2002·Peptides·D A KeireJ R Reeve
Jul 18, 2000·American Journal of Physiology. Gastrointestinal and Liver Physiology·D A KeireJ R Reeve
Nov 7, 2018·Journal of Medicinal Chemistry·Søren ØstergaardBirgitte S Wulff
Jun 6, 2008·Journal of the American Chemical Society·Michael HaackAnnette G Beck-Sickinger

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