DC Field | Value | Language |
---|---|---|
dc.contributor.author | Park, Tae Jung | ko |
dc.contributor.author | Zheng, Shun | ko |
dc.contributor.author | Kang, Yeon Jae | ko |
dc.contributor.author | Lee, SangYup | ko |
dc.date.accessioned | 2010-11-29T05:38:00Z | - |
dc.date.available | 2010-11-29T05:38:00Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2009-04 | - |
dc.identifier.citation | FEMS MICROBIOLOGY LETTERS, v.293, no.1, pp.141 - 147 | - |
dc.identifier.issn | 0378-1097 | - |
dc.identifier.uri | http://hdl.handle.net/10203/20470 | - |
dc.description.abstract | Cell surface display was used as a strategy to display the gold-binding polypeptide (GBP) fusion protein on the surface of Escherichia coli, and consequently to immobilize the cells on the gold surface. The DNA encoding the GBP was fused to the truncated fadL gene and was expressed by the tac promoter. For the display of the core streptavidin (cSA) of Streptomyces avidinii, the cSA gene was fused to the truncated oprF gene. After the dual display of FadL-GBP and OprF-cSA on the surface of E. coli, binding of cells on the gold surface and the interaction of OprF-cSA with the biotin-horseradish peroxidase (HRP) were studied by surface plasmon resonance (SPR) analysis. Cells displaying the FadL-GBP fusion protein could be immobilized on the SPR sensor chip as shown by the SPR angle shift of 0.5 degrees, which was stably bound at least for 60 h with a washing solution. When the FadL-GBP and OprF-cSA fusion proteins were displayed on the same cell surface, the former was used to immobilize the cells on the gold surface and the latter was used for the interaction studies with the biotin-HRP, which demonstrates that the strategy should be useful for developing whole-cell biosensor chips. | - |
dc.description.sponsorship | This work was supported in part by the IT Leading R&D Support Project from the Ministry of Knowledge Economy through IITA. Additional support from the LG Chem Chair Professorship and the KOSEF through the Center for Ultramicrochemical Process Systems are appreciated. We would like to thank Dr S.H. Lee for comments on gene cloning of fadL and oprF. | en |
dc.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | WILEY-BLACKWELL PUBLISHING | - |
dc.title | Development of a whole-cell biosensor by cell surface display of a gold-binding polypeptide on the gold surface | - |
dc.type | Article | - |
dc.identifier.wosid | 000263752000020 | - |
dc.identifier.scopusid | 2-s2.0-61449133142 | - |
dc.type.rims | ART | - |
dc.citation.volume | 293 | - |
dc.citation.issue | 1 | - |
dc.citation.beginningpage | 141 | - |
dc.citation.endingpage | 147 | - |
dc.citation.publicationname | FEMS MICROBIOLOGY LETTERS | - |
dc.contributor.localauthor | Lee, SangYup | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | cell surface display | - |
dc.subject.keywordAuthor | dual display | - |
dc.subject.keywordAuthor | immobilization | - |
dc.subject.keywordAuthor | Escherichia coli | - |
dc.subject.keywordAuthor | surface plasmon resonance | - |
dc.subject.keywordAuthor | gold-binding polypeptide | - |
dc.subject.keywordPlus | MOLECULAR-DYNAMICS SIMULATIONS | - |
dc.subject.keywordPlus | PLASMON RESONANCE | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | ANCHORING MOTIF | - |
dc.subject.keywordPlus | PEPTIDE | - |
dc.subject.keywordPlus | LIPASE | - |
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