Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.peptides.2005.11.018
Title: Structural analysis of peptides that interact with Newcastle disease virus
Authors: Chia, S.L.
Tan, W.S.
Shaari, K.
Abdul Rahman, N.
Yusoff, K.
Satyanarayanajois, S.D. 
Keywords: β-Turn
Alanine-substitution
Circular dichroism
Filamentous M13 bacteriophage
Molecular modeling
Mutagenesis
Newcastle disease virus
Issue Date: Jun-2006
Source: Chia, S.L., Tan, W.S., Shaari, K., Abdul Rahman, N., Yusoff, K., Satyanarayanajois, S.D. (2006-06). Structural analysis of peptides that interact with Newcastle disease virus. Peptides 27 (6) : 1217-1225. ScholarBank@NUS Repository. https://doi.org/10.1016/j.peptides.2005.11.018
Abstract: A peptide with the sequence CTLTTKLYC has previously been identified to inhibit the propagation of Newcastle disease virus (NDV) in embryonated chicken eggs and tissue culture. NDV has been classified into two main groups: the velogenic group, and mesogenic with lentogenic strains as the other group based on its dissociation constants. In this study the peptide, CTLTTKLYC, displayed on the pIII protein of a filamentous M13 phage was synthesized and mutated in order to identify the amino acid residues involved in the interactions with NDV. Mutations of C1 and K6 to A1 and A6 did not affect the binding significantly, but substitution of Y8 with A8 dramatically reduced the interaction. This suggests that Y8 plays an important role in the peptide-virus interaction. The three-dimensional structure of the peptide was determined using circular dichroism (CD), nuclear magnetic resonance (NMR), and molecular modeling. The peptide exhibited two possible conformers. One that consists of consecutive β-turns around T2-L3-T4-T5 and K6-L7-Y8-C9. The other conformer exhibited a β-hairpin bend type of structure with a bend around L3-T4-T5-K6. © 2005 Elsevier Inc. All rights reserved.
Source Title: Peptides
URI: http://scholarbank.nus.edu.sg/handle/10635/106363
ISSN: 01969781
DOI: 10.1016/j.peptides.2005.11.018
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