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Selection of high affinity ligands to hepatitis B core antigen from a phage-displayed cyclic peptide library.


Citation

Ho, Kok Lian and Yusoff, Khatijah and Seow, Heng Fong and Tan, Wen Siang (2003) Selection of high affinity ligands to hepatitis B core antigen from a phage-displayed cyclic peptide library. Journal of Medical Virology, 69 (1). pp. 27-32. ISSN 0146-6615, ESSN: 1096-9071

Abstract

M13 phages that display random disulfide constrained heptapeptides on their gpIII proteins were used to select for high affinity ligands to hepatitis B core antigen (HBcAg). Phages bearing the amino acid sequences C-WSFFSNI-C and C-WPFWGPW-C were isolated, and a binding assay in solution showed that these phages bind tightly to full-length and truncated HBcAg with KDrel values less than 25 nM, which is at least 10 orders of magnitude higher than phage carrying the peptide sequence LLGRMK selected from a linear peptide library. Both the phages that display the constrained peptides were inhibited from binding to HBcAg particles by a monoclonal antibody that binds specifically to the immunodominant region of the particles. A synthetic heptapeptide with the amino acid sequence WSFFSNI derived from one of the fusion peptides inhibits the binding of large surface antigen (L-HBsAg) to core particles with an IC50 value of 12 ± 2 μM. This study has identified a smaller peptide with a greater inhibitory effect on L-HBsAg-HBcAg association.


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Additional Metadata

Item Type: Article
Subject: Hepatitis associated antigen.
Subject: Peptides - Physiological effect.
Divisions: Faculty of Medicine and Health Science
DOI Number: https://doi.org/10.1002/jmv.10266
Publisher: Wiley-Blackwell
Keywords: Biopanning; Dissociation constant; Filamentous phage; HBV assembly; Inhibition study
Depositing User: Raja Norazlinda Raja Azenam
Date Deposited: 14 May 2013 06:36
Last Modified: 17 Sep 2015 04:34
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1002/jmv.10266
URI: http://psasir.upm.edu.my/id/eprint/16650
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