Surface plasmon resonance imaging protein arrays for analysis of triple protein interactions of HPV, E6, E6AP, and p53 = HPV, E6, E6AP, p53 상호작용 연구를 위한 SPR 이미징 단백질 어레이

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Title
Surface plasmon resonance imaging protein arrays for analysis of triple protein interactions of HPV, E6, E6AP, and p53 = HPV, E6, E6AP, p53 상호작용 연구를 위한 SPR 이미징 단백질 어레이
Author(s)
H-S Ro; Byung Hoon Koh; Sun Ok Jung; Hyun Kyu Park; Yong Beom Shin; Min-Gon Kim; Bong Hyun Chung
Bibliographic Citation
Proteomics, vol. 6, no. 7, pp. 2108-2111
Publication Year
2006
Abstract
We have developed a surface plasmon resonance (SPR)-based protein microarray to study protein-protein interactions in a high-throughput mode. As a model system, triple protein interactions have been explored with human papillomaviral E6 protein, tumor suppressor p53, and ubiquitin ligase E6AP. Human papillomavirus (HPV) is known to be a causative agent of cervical cancer. Upon infection, the viral E6 protein forms a heterotrimeric protein complex with p53 and E6AP. The formation of the complex eventually results in the degradation of p53. In the present study, a GST-fused E6AP protein was layered onto a glutathione (GSH)-modified gold chip surface. The specific binding of GST-E6AP protein onto the gold chip surface was facilitated through the affinity of GST to its specific ligand GSH. The interacting proteins (E6 and/or p53) were then spotted. Detection of the interaction was performed using a SPR imaging (SPRI) technique. The resulting SPRI intensity data showed that the protein-protein interactions of E6AP, E6, and p53 were detected in a concentration-dependent manner, suggesting that the SPRI-based microarray system can be an effective tool to study protein-protein interactions where multiple proteins are involved.
Keyword
human papillomavirus (HPV)protein arraysprotein interactionsurface plasmon resonance imaging
ISSN
1615-9853
Publisher
Wiley
DOI
http://dx.doi.org/10.1002/pmic.200500635
Type
Article
Appears in Collections:
Division of Research on National Challenges > Bionanotechnology Research Center > 1. Journal Articles
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