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Title 

Analysis of recombinant protein expression using localized surface plasmon resonance (LSPR)

Authors 

Yong Beom ShinJeong-Min LeeM R ParkMin-Gon KimBong Hyun ChungH B PyoS Maeng

Publisher 

Elsevier

Issue Date 

2007

Citation 

Biosensors & Bioelectronics, vol. 22, no. 9, pp. 2301-2307

Keywords 

affinity-tagged proteinattenuated total reflectiongold nano-islandlabel-free assaylocalized surface plasmon resonance (LSPR)well chipproteinssurface plasmon resonanceaffinity tagged proteinprotein analysis

Abstract 

The localized surface plasmon resonance (LSPR)-based optical biosensor using nano-structures of noble metals has been considered as a useful tool for label-free detection of DNA hybridization and protein-protein interactions. We fabricated LSPR-based optical biosensors using gold nano-islands (nominal thickness; 75 ?) on glass substrates that were easily made using the conventional fabrication methods. The formation of gold nano-islands on glass substrates was realized by heat treatment of thin gold film deposited with a low deposition rate (∼0.05 ?/s). The morphologies of sensor surfaces composed of gold nano-islands were observed using an atomic force microscope (AFM) with a non-contact mode. To investigate the sensing capacity of the gold nano-island sensor for the binding of proteins by affinity interactions, the streptavidin and biotin interaction was used as a model system. In addition, detection of recombinant glutathione-S-transferase (GST)-tagged human interleukin-6 (hIL6) expressed in Escherichia coli was carried out by LSPR. It is expected that the LSPR sensors composed of gold nano-islands can be an alternative to traditional methods such as SDS-polyacrylamide gel electrophoresis (SDS-PAGE) for fast analysis of protein expression.

ISSN 

0956-5663

Link 

http://dx.doi.org/10.1016/j.bios.2006.12.028

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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