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Sensing of p53 and EGFR Biomarkers Using High Efficiency SERS Substrates

In this paper we describe a method for the determination of protein concentration using Surface Enhanced Raman Resonance Scattering (SERRS) immunoassays. We use two different Raman active linkers, 4-aminothiophenol and 6-mercaptopurine, to bind to a high sensitivity SERS substrate and investigate th...

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Detalles Bibliográficos
Autores principales: Owens, Peter, Phillipson, Nigel, Perumal, Jayakumar, O’Connor, Gerard M., Olivo, Malini
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4697139/
https://www.ncbi.nlm.nih.gov/pubmed/26516922
http://dx.doi.org/10.3390/bios5040664
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author Owens, Peter
Phillipson, Nigel
Perumal, Jayakumar
O’Connor, Gerard M.
Olivo, Malini
author_facet Owens, Peter
Phillipson, Nigel
Perumal, Jayakumar
O’Connor, Gerard M.
Olivo, Malini
author_sort Owens, Peter
collection PubMed
description In this paper we describe a method for the determination of protein concentration using Surface Enhanced Raman Resonance Scattering (SERRS) immunoassays. We use two different Raman active linkers, 4-aminothiophenol and 6-mercaptopurine, to bind to a high sensitivity SERS substrate and investigate the influence of varying concentrations of p53 and EGFR on the Raman spectra. Perturbations in the spectra are due to the influence of protein–antibody binding on Raman linker molecules and are attributed to small changes in localised mechanical stress, which are enhanced by SERRS. These influences are greatest for peaks due to the C-S functional group and the Full Width Half Maximum (FWHM) was found to be inversely proportional to protein concentration.
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spelling pubmed-46971392016-01-19 Sensing of p53 and EGFR Biomarkers Using High Efficiency SERS Substrates Owens, Peter Phillipson, Nigel Perumal, Jayakumar O’Connor, Gerard M. Olivo, Malini Biosensors (Basel) Article In this paper we describe a method for the determination of protein concentration using Surface Enhanced Raman Resonance Scattering (SERRS) immunoassays. We use two different Raman active linkers, 4-aminothiophenol and 6-mercaptopurine, to bind to a high sensitivity SERS substrate and investigate the influence of varying concentrations of p53 and EGFR on the Raman spectra. Perturbations in the spectra are due to the influence of protein–antibody binding on Raman linker molecules and are attributed to small changes in localised mechanical stress, which are enhanced by SERRS. These influences are greatest for peaks due to the C-S functional group and the Full Width Half Maximum (FWHM) was found to be inversely proportional to protein concentration. MDPI 2015-10-28 /pmc/articles/PMC4697139/ /pubmed/26516922 http://dx.doi.org/10.3390/bios5040664 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Owens, Peter
Phillipson, Nigel
Perumal, Jayakumar
O’Connor, Gerard M.
Olivo, Malini
Sensing of p53 and EGFR Biomarkers Using High Efficiency SERS Substrates
title Sensing of p53 and EGFR Biomarkers Using High Efficiency SERS Substrates
title_full Sensing of p53 and EGFR Biomarkers Using High Efficiency SERS Substrates
title_fullStr Sensing of p53 and EGFR Biomarkers Using High Efficiency SERS Substrates
title_full_unstemmed Sensing of p53 and EGFR Biomarkers Using High Efficiency SERS Substrates
title_short Sensing of p53 and EGFR Biomarkers Using High Efficiency SERS Substrates
title_sort sensing of p53 and egfr biomarkers using high efficiency sers substrates
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4697139/
https://www.ncbi.nlm.nih.gov/pubmed/26516922
http://dx.doi.org/10.3390/bios5040664
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