![]() |
|
|
JF Goossens, N Pommery, M Lohez, J Pommery, N Helbecque, P Cotelle, M Lhermitte and JP Henichart
INSERM U 16, Lille, France.
The conformation of various regions of vasoactive intestinal peptide (VIP) has been analyzed by semiempirical methods, CD, and NMR spectroscopy, indicating that residues 11-21 are most likely to be helical, whereas the amino-terminal portion VIP(1-11) could exhibit two beta-turn structures. VIP(1-11) inhibits 125I-VIP binding to intact guinea pig tracheal epithelial cells and the VIP-induced smooth muscle response. However, the endecapeptide exhibits no effect on the muscle tone. All these data suggest that VIP(1-11) may be a useful tool in studying VIP receptor recognition, its regulation, and cellular functions.
This article has been cited by other articles:
![]() |
H. Igarashi, T. Ito, T. K. Pradhan, S. A. Mantey, W. Hou, D. H. Coy, and R. T. Jensen Elucidation of the Vasoactive Intestinal Peptide Pharmacophore for VPAC2 Receptors in Human and Rat and Comparison to the Pharmacophore for VPAC1 Receptors J. Pharmacol. Exp. Ther., November 1, 2002; 303(2): 445 - 460. [Abstract] [Full Text] [PDF] |
||||