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A Novel Strategy for Analyzing RNA-Protein Interactions by Surface Plasmon Resonance Biosensor

Surface plasmon resonance (SPR) biosensor is a promising technology for its various advantages including the real-time measurement of biomolecular interactions without labeling. A method of hybridizing RNAs on the surface of the streptavidin-coated (SA) sensor chip to study RNA-protein interactions...

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Detalles Bibliográficos
Autores principales: Yang, Yaling, Wang, Quan, Guo, Deyin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Humana Press Inc 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7090661/
https://www.ncbi.nlm.nih.gov/pubmed/18465270
http://dx.doi.org/10.1007/s12033-008-9066-3
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author Yang, Yaling
Wang, Quan
Guo, Deyin
author_facet Yang, Yaling
Wang, Quan
Guo, Deyin
author_sort Yang, Yaling
collection PubMed
description Surface plasmon resonance (SPR) biosensor is a promising technology for its various advantages including the real-time measurement of biomolecular interactions without labeling. A method of hybridizing RNAs on the surface of the streptavidin-coated (SA) sensor chip to study RNA-protein interactions was described in this paper. In our study, it has been shown that the nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) has a high binding affinity for the leader sequence of SARS-CoV genome. Effect of temperature on the RNA-DNA hybridization was also examined. This method can provide the affinity of interactions with high sensitivity. Therefore, it will be useful in screening binding candidates for a given RNA target motif with one chip.
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spelling pubmed-70906612020-03-24 A Novel Strategy for Analyzing RNA-Protein Interactions by Surface Plasmon Resonance Biosensor Yang, Yaling Wang, Quan Guo, Deyin Mol Biotechnol Research Surface plasmon resonance (SPR) biosensor is a promising technology for its various advantages including the real-time measurement of biomolecular interactions without labeling. A method of hybridizing RNAs on the surface of the streptavidin-coated (SA) sensor chip to study RNA-protein interactions was described in this paper. In our study, it has been shown that the nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) has a high binding affinity for the leader sequence of SARS-CoV genome. Effect of temperature on the RNA-DNA hybridization was also examined. This method can provide the affinity of interactions with high sensitivity. Therefore, it will be useful in screening binding candidates for a given RNA target motif with one chip. Humana Press Inc 2008-05-09 2008 /pmc/articles/PMC7090661/ /pubmed/18465270 http://dx.doi.org/10.1007/s12033-008-9066-3 Text en © Humana Press 2008 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Research
Yang, Yaling
Wang, Quan
Guo, Deyin
A Novel Strategy for Analyzing RNA-Protein Interactions by Surface Plasmon Resonance Biosensor
title A Novel Strategy for Analyzing RNA-Protein Interactions by Surface Plasmon Resonance Biosensor
title_full A Novel Strategy for Analyzing RNA-Protein Interactions by Surface Plasmon Resonance Biosensor
title_fullStr A Novel Strategy for Analyzing RNA-Protein Interactions by Surface Plasmon Resonance Biosensor
title_full_unstemmed A Novel Strategy for Analyzing RNA-Protein Interactions by Surface Plasmon Resonance Biosensor
title_short A Novel Strategy for Analyzing RNA-Protein Interactions by Surface Plasmon Resonance Biosensor
title_sort novel strategy for analyzing rna-protein interactions by surface plasmon resonance biosensor
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7090661/
https://www.ncbi.nlm.nih.gov/pubmed/18465270
http://dx.doi.org/10.1007/s12033-008-9066-3
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