Examination of the role of the amphipathic alpha -helix in the interaction of neuropeptide Y and active cyclic analogues with cell membrane receptors and dimyristoylphosphatidyl-choline

To test the potential importance of the putative C-terminal amphipathic alpha -helical region of neuropeptide Y (NPY) in receptor binding, the interactions of porcine NPY and several peptide analogues with lipid and cell membrane receptors were compared. Data from fluorescence, differential scanning...

Full description

Saved in:
Bibliographic Details
Published in:Biochemistry (Easton) 1990-01, Vol.29 (8), p.2016-2022
Main Authors: McLean, L R, Buck, SH, Krstenansky, J L
Format: Article
Language:English
Subjects:
dimyristoylphosphatidylcholine
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:To test the potential importance of the putative C-terminal amphipathic alpha -helical region of neuropeptide Y (NPY) in receptor binding, the interactions of porcine NPY and several peptide analogues with lipid and cell membrane receptors were compared. Data from fluorescence, differential scanning calorimetry, and liposome clearing experiments suggest that, although the interaction of NPY with lipid is consistent with formation of an amphipathic alpha -helix, a simple amphipathic alpha -helical model for the interaction with the high-affinity NPY receptor is insufficient to explain the data. Rather, the data suggest that the amphipathic alpha -helix in NPY plays a significant role in stabilizing the spatial relationship between the N- and C-terminal residues of the peptide when bound to its receptor.
ISSN:0006-2960