Rapid detection of aflatoxin B-1 by a bifunctional protein crosslinker-based surface plasmon resonance biosensor
- Authors
- Park, Jae Hong; Kim, Young-Pi; Kim, In-Ho; Ko, Sungho
- Issue Date
- Feb-2014
- Publisher
- ELSEVIER SCI LTD
- Keywords
- Bifunctional protein crosslinker; Gold substrate; Immunosensor; Aflatoxin B-1; Self-assembled monolayer; Thiolated chemical linker
- Citation
- FOOD CONTROL, v.36, no.1, pp.183 - 190
- Indexed
- SCIE
SCOPUS
- Journal Title
- FOOD CONTROL
- Volume
- 36
- Number
- 1
- Start Page
- 183
- End Page
- 190
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/160708
- DOI
- 10.1016/j.foodcont.2013.08.038
- ISSN
- 0956-7135
- Abstract
- The aim of this study was the development of a bifunctional protein crosslinker-based surface plasmon resonance (SPR) biosensor for rapid detection of aflatoxin B-1 (AFB(1)), a potent carcinogen. A fusion protein was obtained by genetically fusing gold binding protein (GBP) that binds strongly to gold surfaces to protein G (ProG) that interacts with the Fc portion of antibodies. It was used as a bifunctional crosslinker for rapid self-oriented immobilization of antibodies on gold substrates without any chemical treatment. SPR analyses demonstrated the binding of the GBP-ProG crosslinker to the gold surface was superior to that of an only ProG via currently used self-assembled monolayers of alkanethiol due to the GBP property. As a result, anti-AFB(1) antibodies were 36% more immobilized on the GBP-ProG layer than the ProG layer. When the GBP-ProG crosslinker-based SPR chips were fabricated with the best density (100 mu g/mL) of anti-AFB(1) antibodies, they could detect AFB(1) as low as 1 mu g/mL in both buffer and corn extracts and selectively detect it with negligible SPR responses in control toxins (zearalenone and ochratoxin A). These results mean the GBP-ProG is more useful than the thiolated chemical linkers for development of gold substrate-based immunosensors, and this GBP-ProG crosslinker-based immunosensor could detect small molecules effectively.
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