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Selection of high affinity ligands to hepatitis B core antigen from a phage‐displayed cyclic peptide library
Author(s) -
Ho Kok Lian,
Yusoff Khatijah,
Seow Heng Fong,
Tan Wen Siang
Publication year - 2003
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.10266
Subject(s) - hbcag , phage display , peptide , hbsag , monoclonal antibody , antigen , microbiology and biotechnology , peptide library , peptide sequence , virology , amino acid , epitope , antibody , biology , chemistry , hepatitis b virus , biochemistry , virus , gene , genetics
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 relvalues 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 IC 50 value of 12 ± 2 μM. This study has identified a smaller peptide with a greater inhibitory effect on L‐HBsAg‐HBcAg association. J. Med. Virol. 69:27–32, 2003. © 2003 Wiley‐Liss, Inc.