Please use this identifier to cite or link to this item:
|Title:||Conformation of neuropeptide Y receptor antagonists: Structural implications in receptor selectivity|
|Authors:||Jois, S.D.S. |
|Source:||Jois, S.D.S., Balasubramaniam, A. (2003-07-01). Conformation of neuropeptide Y receptor antagonists: Structural implications in receptor selectivity. Peptides 24 (7) : 1035-1043. ScholarBank@NUS Repository. https://doi.org/10.1016/S0196-9781(03)00183-9|
|Abstract:||Two NPY analogue peptides, BVD10 (Ile-Asn-Pro-Ile-Tyr-Arg-Leu-Arg-Tyr-OMe) and BVD15 (Ile-Asn-Pro-Ile-Tyr-Arg-Leu-Arg-Tyr-NH2) were characterized conformationally by NMR, CD and molecular dynamics simulations. The two peptides exhibit different secondary structure characteristics in trifluoroethanol. BVD10 exhibits a structure with two consecutive β-turns at Asn2-Pro3-Ile4-Tyr5 and Ile4-Tyr5-Arg6-Leu7. BVD15 exhibits a helical type of structure along with a β-turn at Asn2-Pro3-Ile4-Tyr5. Molecular modeling studies suggested that the C-terminus Tyr9 is oriented in different directions in the two peptides. The difference in the structures of peptides observed may contribute to the Y1 selectivity of BVD10 relative to BVD15. © 2003 Elsevier Inc. All rights reserved.|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Feb 22, 2018
WEB OF SCIENCETM
checked on Jan 23, 2018
checked on Feb 19, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.