Characterization of a Bacterial Self-Assembly Surface Layer Protein and Its Application as an Electrical Nanobiosensor
- Authors
- Park, Tae Jung; Lee, Seok Jae; Park, Jong Pil; Yang, Min Ho; Choi, Jong Hyun; Lee, Sang Yup
- Issue Date
- Jan-2011
- Publisher
- AMER SCIENTIFIC PUBLISHERS
- Keywords
- Surface Layer Protein; Single-Walled Carbon Nanotubes Array; Self-Assembled Nanocomplex; Streptavidin-Biotin Interaction; Electronic Biosensor
- Citation
- JOURNAL OF NANOSCIENCE AND NANOTECHNOLOGY, v.11, no.1, pp 402 - 407
- Pages
- 6
- Journal Title
- JOURNAL OF NANOSCIENCE AND NANOTECHNOLOGY
- Volume
- 11
- Number
- 1
- Start Page
- 402
- End Page
- 407
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/27732
- DOI
- 10.1166/jnn.2011.3264
- ISSN
- 1533-4880
1533-4899
- Abstract
- Bacterial cell surface layers (S-layers) are one of the most common outermost cell envelope components of prokaryotic organisms (Archaea and bacteria), which can self-assemble into two-dimensional (2D) crystalline arrays. Production and characterization of the bacterial S-layer protein (SLP) from Geobacillus stearothermophilus, a thermophilic bacterium, are demonstrated in this study. Based on this, purified SLPs were applied for wrapping around single-walled carbon nanotubes (CNTs) and applying as electrochemical sensing tools. For the large scale production of SLP, fed-batch culture of G. stearothermophilus was carried out by DO-stat strategy. Purified SLPs were characterized by atomic force microscopy (AFM). After recrystallization of purified SLPs with gold colloids, the formation of two-dimensional (2D) oblique lattice was observed by transmission electron microscopy (TEM). Metallic or near metallic characteristics of CNTs were measured by current voltage (I-V) analyzer. By high-cell density cultivation, cells grew to 10 g/l of dry cell weight in 65 h and the S-layer contents were achieved up to 40% of total proteins. The SLPs were purified to electrophoretic homogeneity and the molecular mass was estimated to be about 105 kDa. The purified SLPs were self-assembled and confirmed their hexagonal symmetry lattice structure. The SLP subunits were cross-linked to each other and to the underlying CNTs by non-covalent interaction, which was caused to change the electric current between natural CNTs and SLP-wrapped CNTs. One-dimensional structure and large aspect ratio of the functionalized CNTs may allow effective targeting of biomolecules by specific binding, such as protein-protein, DNA-DNA, and protein-ligand interaction. Bacterial SLP could be used as a biological template for immobilization molecular array, and provides new approaches for nanoelectronic biosensor applications.
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Collections - College of Natural Sciences > Department of Chemistry > 1. Journal Articles
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