Predicting interactive behavior of cytokines and their receptors by dielectric thermal analysis and thermogravimetry
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  • 作者:Susan Moreno-Molek (1)
    Salaam Saleh (1)
    Druthiman Reddy Mantheni (2)
    Manik Pavan Kumar Maheswaram (2)
    Tobili Sam-Yellowe (1) t.sam-yellowe@csuohio.edu
    Alan T. Riga (2) a.riga@csuohio.edu
  • 关键词:Dielectric thermal analysis &#8211 ; Thermogravimetric analysis &#8211 ; Cytokines &#8211 ; Cytokine receptors &#8211 ; Malaria &#8211 ; Electrical conductivity &#8211 ; Plasmodium falciparum
  • 刊名:Journal of Thermal Analysis and Calorimetry
  • 出版年:2012
  • 出版时间:April 2012
  • 年:2012
  • 卷:108
  • 期:1
  • 页码:79-85
  • 全文大小:365.3 KB
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  • 作者单位:1. Department of Biological, Geological, and Environmental Sciences, Cleveland State University, Cleveland, OH 44115, USA2. Department of Chemistry, Cleveland State University, Cleveland, OH 44115, USA
  • 刊物类别:Chemistry and Materials Science
  • 刊物主题:Chemistry
    Sciences
    Polymer Sciences
    Physical Chemistry
    Inorganic Chemistry
    Measurement Science and Instrumentation
  • 出版者:Akad茅miai Kiad贸, co-published with Springer Science+Business Media B.V., Formerly Kluwer Academic
  • ISSN:1572-8943
文摘
Cytokines and soluble cytokine receptors serve as important protein biomarkers for chronic and infectious disease diagnosis. The development of biosensors capable of detecting cytokines or their soluble receptors in patient bodily fluids is a growing area of research. In an ongoing series of studies to understand the thermal analytical behavior of cytokines and their soluble receptors, dielectric thermal analysis (DETA) and thermogravimetry (TG) were used in investigations to determine if differentiations based on dielectric properties (e.g., conductivity) of the proteins could be identified. Permittivity (ε′) and dielectric loss factor (ε″) measurements were performed over a frequency range of 0.1–300,000 Hz. Up to 20 min, water associated with the samples was conductive, interacting with the proteins and affecting the temperature-dependent relaxation spectra of proteins. A trend analysis revealed differences between surface charge at 0.1 Hz and bulk charge at 300,000 Hz. In addition, the greatest change detected among proteins was due to the conductivity (dielectric loss factor). Beyond a 20 min drying time, the observed conductivity was due to intrinsic properties of the proteins with limited dependence on frequency. A 100% water loss was obtained for samples within 20–30 min by TG. Sample drying by TG could serve as a preparatory step in drying protein samples for further DETA and DSC analysis.

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