Two-Dimensional Fluorescence Difference Spectroscopy of ZnO and Mg Composites in the Detection of Physiological Protein and RNA Interactions
by
Amanda Hoffman 1, Xiaotong Wu 1, Jianjie Wang 2, Amanda Brodeur 2, Rintu Thomas 2, Ravindra Thakkar 1, Halena Hadi 3, Garry P. Glaspell 4, Molly Duszynski 5, Adam Wanekaya 5 and Robert K. DeLong 1,*
Amanda Hoffman 1, Xiaotong Wu 1, Jianjie Wang 2, Amanda Brodeur 2, Rintu Thomas 2, Ravindra Thakkar 1, Halena Hadi 3, Garry P. Glaspell 4, Molly Duszynski 5, Adam Wanekaya 5 and Robert K. DeLong 1,*
1
Department of Anatomy and Physiology, Nanotechnology Innovation Center of Kansas State (NICKS), Kansas State University, Manhattan, KS 66506, USA
2
Department of Biomedical Science, Missouri State University, Springfield, MO 65897, USA
3
University of Notre Dame, Notre Dame, IN 46556, USA
4
Department of Chemistry, Virginia Commonwealth University, Richmond, VA 23284, USA
5
Department of Chemistry, Missouri State University, Springfield, MO 65897, USA
*
Author to whom correspondence should be addressed.
Materials 2017, 10(12), 1430; https://doi.org/10.3390/ma10121430
Received: 31 October 2017 / Revised: 7 December 2017 / Accepted: 8 December 2017 / Published: 15 December 2017
(This article belongs to the Special Issue Zinc Oxide Nanostructures: Synthesis and Characterization)
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.
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Keywords:
zinc oxide; nanocomposites; aptamer; thrombin; angiotensin-converting enzyme; ribonuclease A; RNA; two-dimensional fluorescence difference spectroscopy
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MDPI and ACS Style
Hoffman, A.; Wu, X.; Wang, J.; Brodeur, A.; Thomas, R.; Thakkar, R.; Hadi, H.; Glaspell, G.P.; Duszynski, M.; Wanekaya, A.; DeLong, R.K. Two-Dimensional Fluorescence Difference Spectroscopy of ZnO and Mg Composites in the Detection of Physiological Protein and RNA Interactions. Materials 2017, 10, 1430.
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