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Development of virus nanoparticles for sensitive antibody detection via genetic and unnatural amino acid modification of the coat proteins
- Alternative Title
- Development of virus nanoparticles for sensitive antibody detection via genetic and unnatural amino acid modification of the coat proteins
- Author(s)
- 신승건
- Alternative Author(s)
- seunggun shin
- Advisor
- 유태현
- Department
- 일반대학원 분자과학기술학과
- Publisher
- The Graduate School, Ajou University
- Publication Year
- 2016-02
- Language
- eng
- Keyword
- immuno pcr; phage display; antigen detection
- Alternative Abstract
- The virus particle has attractive features as materials, for example, homogenous size, specific modifications of particle surface via genetic and chemical manipulations, and self-amplification via its own genetic information. These properties make researchers try to develop biomaterials, sensor and scaffolds based on phage. Detection by immuno-PCR exhibits high sensitivity, but it usually requires a complex manufacturing process especially for protein-DNA conjugates. We anticipated that a genetically modified M13 bacteriophage can be used as a detection molecule in immuno-PCR. In this study, we have developed a novel bacteriophage particle which displays Z domain, an IgG binding protein, at the pIII coat proteins. The virus particle has not only a template for PCR but also a binding capability to IgG; thus the new sensing reagent can be used for immune-PCR directly by itself. The cTnI myocardial infarction marker is chosen for the demonstration of an immuno-PCR assay method using the modified bacteriophage. An initially developed immuno-PCR method showed a limit of detection as 0.092 ng cTnI/mL, which is about 4-fold lower than an ELISA method. In order to improve the platform, we are applying the site-specific modification strategies using unnatural amino acids by incorporating the analogues into the pIII and/or pVIII coat proteins. For an example, we are developing a simple method to conjugate IgG to the Z domain-displayed phage particle via a light-mediated reaction.
- Fulltext
- Appears in Collections:
- Graduate School of Ajou University > Department of Molecular Science and Technology > 3. Theses(Master)
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