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 0146-6615Full text for this resource is not available from the Research Repository.
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.
|Uncontrolled Keywords:||ResPubID19030, biopanning, filamentous phage, dissociation constant, inhibition study, HBV assembly|
|Subjects:||Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences|
|Date Deposited:||23 Feb 2012 01:05|
|Last Modified:||20 Jan 2015 22:56|
|ePrint Statistics:||View download statistics for this item|
|Citations in Scopus:||24 - View on Scopus|
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