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Selection of High Affinity Ligands to Hepatitis B Core Antigen From a Phage-Displayed Cyclic Peptide Library

Hoy, K and Yusoff, Khatijah and Seow, Heng-Fong and Tan, Wen Siang (2004) 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

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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 K D rel 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 microM. This study has identified a smaller peptide with a greater inhibitory effect on L-HBsAg-HBcAg association.

Item Type: Article
Uncontrolled Keywords: ResPubID19030, biopanning, filamentous phage, dissociation constant, inhibition study, HBV assembly
Subjects: Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Depositing User: VUIR
Date Deposited: 23 Feb 2012 01:05
Last Modified: 20 Jan 2015 22:56
URI: http://vuir.vu.edu.au/id/eprint/2596
DOI: 10.1002/jmv.10266
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Citations in Scopus: 24 - View on Scopus

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