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Two-Dimensional Fluorescence Difference Spectroscopy of ZnO and Mg Composites in the Detection of Physiological Protein and RNA Interactions
Two-dimensional fluorescence difference spectroscopy (2-D FDS) was used to determine the unique spectral signatures of zinc oxide (ZnO), magnesium oxide (MgO), and 5% magnesium zinc oxide nanocomposite (5% Mg/ZnO) and was then used to demonstrate the change in spectral signature that occurs when phy...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5744365/ https://www.ncbi.nlm.nih.gov/pubmed/29244716 http://dx.doi.org/10.3390/ma10121430 |
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author | Hoffman, Amanda Wu, Xiaotong Wang, Jianjie Brodeur, Amanda Thomas, Rintu Thakkar, Ravindra Hadi, Halena Glaspell, Garry P. Duszynski, Molly Wanekaya, Adam DeLong, Robert K. |
author_facet | Hoffman, Amanda Wu, Xiaotong Wang, Jianjie Brodeur, Amanda Thomas, Rintu Thakkar, Ravindra Hadi, Halena Glaspell, Garry P. Duszynski, Molly Wanekaya, Adam DeLong, Robert K. |
author_sort | Hoffman, Amanda |
collection | PubMed |
description | Two-dimensional fluorescence difference spectroscopy (2-D FDS) was used to determine the unique spectral signatures of zinc oxide (ZnO), magnesium oxide (MgO), and 5% magnesium zinc oxide nanocomposite (5% Mg/ZnO) and was then used to demonstrate the change in spectral signature that occurs when physiologically important proteins, such as angiotensin-converting enzyme (ACE) and ribonuclease A (RNase A), interact with ZnO nanoparticles (NPs). When RNase A is bound to 5% Mg/ZnO, the intensity is quenched, while the intensity is magnified and a significant shift is seen when torula yeast RNA (TYRNA) is bound to RNase A and 5% Mg/ZnO. The intensity of 5% Mg/ZnO is quenched also when thrombin and thrombin aptamer are bound to the nanocomposite. These data indicate that RNA–protein interaction can occur unimpeded on the surface of NPs, which was confirmed by gel electrophoresis, and importantly that the change in fluorescence excitation, emission, and intensity shown by 2-D FDS may indicate specificity of biomolecular interactions. |
format | Online Article Text |
id | pubmed-5744365 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-57443652017-12-31 Two-Dimensional Fluorescence Difference Spectroscopy of ZnO and Mg Composites in the Detection of Physiological Protein and RNA Interactions Hoffman, Amanda Wu, Xiaotong Wang, Jianjie Brodeur, Amanda Thomas, Rintu Thakkar, Ravindra Hadi, Halena Glaspell, Garry P. Duszynski, Molly Wanekaya, Adam DeLong, Robert K. Materials (Basel) Brief Report Two-dimensional fluorescence difference spectroscopy (2-D FDS) was used to determine the unique spectral signatures of zinc oxide (ZnO), magnesium oxide (MgO), and 5% magnesium zinc oxide nanocomposite (5% Mg/ZnO) and was then used to demonstrate the change in spectral signature that occurs when physiologically important proteins, such as angiotensin-converting enzyme (ACE) and ribonuclease A (RNase A), interact with ZnO nanoparticles (NPs). When RNase A is bound to 5% Mg/ZnO, the intensity is quenched, while the intensity is magnified and a significant shift is seen when torula yeast RNA (TYRNA) is bound to RNase A and 5% Mg/ZnO. The intensity of 5% Mg/ZnO is quenched also when thrombin and thrombin aptamer are bound to the nanocomposite. These data indicate that RNA–protein interaction can occur unimpeded on the surface of NPs, which was confirmed by gel electrophoresis, and importantly that the change in fluorescence excitation, emission, and intensity shown by 2-D FDS may indicate specificity of biomolecular interactions. MDPI 2017-12-15 /pmc/articles/PMC5744365/ /pubmed/29244716 http://dx.doi.org/10.3390/ma10121430 Text en © 2017 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 (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Brief Report Hoffman, Amanda Wu, Xiaotong Wang, Jianjie Brodeur, Amanda Thomas, Rintu Thakkar, Ravindra Hadi, Halena Glaspell, Garry P. Duszynski, Molly Wanekaya, Adam DeLong, Robert K. Two-Dimensional Fluorescence Difference Spectroscopy of ZnO and Mg Composites in the Detection of Physiological Protein and RNA Interactions |
title | Two-Dimensional Fluorescence Difference Spectroscopy of ZnO and Mg Composites in the Detection of Physiological Protein and RNA Interactions |
title_full | Two-Dimensional Fluorescence Difference Spectroscopy of ZnO and Mg Composites in the Detection of Physiological Protein and RNA Interactions |
title_fullStr | Two-Dimensional Fluorescence Difference Spectroscopy of ZnO and Mg Composites in the Detection of Physiological Protein and RNA Interactions |
title_full_unstemmed | Two-Dimensional Fluorescence Difference Spectroscopy of ZnO and Mg Composites in the Detection of Physiological Protein and RNA Interactions |
title_short | Two-Dimensional Fluorescence Difference Spectroscopy of ZnO and Mg Composites in the Detection of Physiological Protein and RNA Interactions |
title_sort | two-dimensional fluorescence difference spectroscopy of zno and mg composites in the detection of physiological protein and rna interactions |
topic | Brief Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5744365/ https://www.ncbi.nlm.nih.gov/pubmed/29244716 http://dx.doi.org/10.3390/ma10121430 |
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