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

Cited 31 time in scopus
Metadata Downloads
Analysis of recombinant protein expression using localized surface plasmon resonance (LSPR)
Yong Beom Shin; Jeong-Min Lee; M R Park; Min-Gon Kim; Bong Hyun Chung; H B Pyo; S Maeng
Bibliographic Citation
Biosensors & Bioelectronics, vol. 22, no. 9, pp. 2301-2307
Publication Year
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.
Affinity-tagged proteinAttenuated total reflectionGold nano-islandLabel-free assayLocalized surface plasmon resonance (LSPR)Well chip
Appears in Collections:
Division of Research on National Challenges > Bionanotechnology Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.

Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.