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...
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my.upm.eprints.166502024-08-05T02:32:23Z http://psasir.upm.edu.my/id/eprint/16650/ Selection of high affinity ligands to hepatitis B core antigen from a phage-displayed cyclic peptide library. Ho, Kok Lian Yusoff, Khatijah Seow, Heng Fong Tan, Wen Siang 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. Wiley-blackwell 2003-01 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/16650/1/Selection%20of%20high%20affinity%20ligands%20to%20hepatitis%20B%20core%20antigen%20from%20a%20phage.pdf text en http://psasir.upm.edu.my/id/eprint/16650/7/Journal%20of%20Medical%20Virology%20-%202002%20-%20Ho%20-%20Selection%20of%20high%20affinity%20ligands%20to%20hepatitis%20B%20core%20antigen%20from%20a.pdf 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 http://as.wiley.com/WileyCDA/Brand/id-35.html Hepatitis associated antigen. Peptides - Physiological effect. 10.1002/jmv.10266 English |
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Hepatitis associated antigen. Peptides - Physiological effect. Ho, Kok Lian Yusoff, Khatijah Seow, Heng Fong Tan, Wen Siang Selection of high affinity ligands to hepatitis B core antigen from a phage-displayed cyclic peptide library. |
description |
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. |
format |
Article |
author |
Ho, Kok Lian Yusoff, Khatijah Seow, Heng Fong Tan, Wen Siang |
author_facet |
Ho, Kok Lian Yusoff, Khatijah Seow, Heng Fong Tan, Wen Siang |
author_sort |
Ho, Kok Lian |
title |
Selection of high affinity ligands to hepatitis B core antigen from a phage-displayed cyclic peptide library. |
title_short |
Selection of high affinity ligands to hepatitis B core antigen from a phage-displayed cyclic peptide library. |
title_full |
Selection of high affinity ligands to hepatitis B core antigen from a phage-displayed cyclic peptide library. |
title_fullStr |
Selection of high affinity ligands to hepatitis B core antigen from a phage-displayed cyclic peptide library. |
title_full_unstemmed |
Selection of high affinity ligands to hepatitis B core antigen from a phage-displayed cyclic peptide library. |
title_sort |
selection of high affinity ligands to hepatitis b core antigen from a phage-displayed cyclic peptide library. |
publisher |
Wiley-blackwell |
publishDate |
2003 |
url |
http://psasir.upm.edu.my/id/eprint/16650/1/Selection%20of%20high%20affinity%20ligands%20to%20hepatitis%20B%20core%20antigen%20from%20a%20phage.pdf http://psasir.upm.edu.my/id/eprint/16650/7/Journal%20of%20Medical%20Virology%20-%202002%20-%20Ho%20-%20Selection%20of%20high%20affinity%20ligands%20to%20hepatitis%20B%20core%20antigen%20from%20a.pdf http://psasir.upm.edu.my/id/eprint/16650/ http://as.wiley.com/WileyCDA/Brand/id-35.html |
_version_ |
1806690460124577792 |
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13.188404 |