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

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.

Preview Text (Abstract) Selection of high affinity ligands to hepatitis B core antigen from a phage.pdf Download (182kB) | Preview Text Journal of Medical Virology - 2002 - Ho - Selection of high affinity ligands to hepatitis B core antigen from a.pdf - Published Version Restricted to Repository staff only Download (178kB) Official URL or Download Paper: http://as.wiley.com/WileyCDA/Brand/id-35.html

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