Citation
Abstract
A disulfide constrained random heptapeptide library displayed on filamentous bacteriophage M13 was applied to select specific ligands that interact with Newcastle disease virus (NDV). A fusion phage carrying the amino acid sequence TLTTKLY was selected from the panning procedure. An antibody competition assay showed that the selected phage was capable of competing with the polyclonal antibodies raised against NDV for binding sites on the virus. Determination of the binding affinity of this phage with NDV by an equilibrium binding assay in solution revealed two different dissociation constants, suggesting that there could be two distinct binding sites for the phage on NDV. Synthetic peptides with the sequence CTLTTKLYC, either in linear or cyclic conformations inhibited the binding of phage bearing the same sequence to NDV. These peptides also inhibited the hemolytic activity of the virus as well as its propagation in embryonated chicken eggs.
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Official URL or Download Paper: https://link.springer.com/article/10.1007/s00705-0...
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Additional Metadata
Item Type: | Article |
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Divisions: | Faculty of Science and Environmental Studies |
DOI Number: | https://doi.org/10.1007/s00705-001-0778-y |
Publisher: | Springer |
Keywords: | Specific ligands; Binding site; Equilibrium binding assay; Hemolytic activity; Novel peptides; Newcastle disease virus; Phage display; Synthetic peptides; TLTTKLY |
Depositing User: | Ms. Zaimah Saiful Yazan |
Date Deposited: | 03 Mar 2025 06:21 |
Last Modified: | 03 Mar 2025 06:21 |
Altmetrics: | http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1007/s00705-001-0778-y |
URI: | http://psasir.upm.edu.my/id/eprint/111867 |
Statistic Details: | View Download Statistic |
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