Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0196-9781(03)00183-9
Title: Conformation of neuropeptide Y receptor antagonists: Structural implications in receptor selectivity
Authors: Jois, S.D.S. 
Balasubramaniam, A.
Keywords: Beta-turn
Helical structure
NMR
NPY peptide
Trifluoroethanol
Issue Date: 1-Jul-2003
Citation: 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.
Source Title: Peptides
URI: http://scholarbank.nus.edu.sg/handle/10635/105772
ISSN: 01969781
DOI: 10.1016/S0196-9781(03)00183-9
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