Authors:
Susan Moreno-Molek Department of Biological, Geological, and Environmental Sciences, Cleveland State University, Cleveland, OH, 44115, USA

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Salaam Saleh Department of Biological, Geological, and Environmental Sciences, Cleveland State University, Cleveland, OH, 44115, USA

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Druthiman Reddy Mantheni Department of Chemistry, Cleveland State University, Cleveland, OH, 44115, USA

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Manik Pavan Kumar Maheswaram Department of Chemistry, Cleveland State University, Cleveland, OH, 44115, USA

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Tobili Sam-Yellowe Department of Biological, Geological, and Environmental Sciences, Cleveland State University, Cleveland, OH, 44115, USA

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Alan T. Riga Department of Chemistry, Cleveland State University, Cleveland, OH, 44115, USA

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Abstract

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 (∊′) and dielectric loss factor (∊″) 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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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation
1969
Volumes
per Year
1
Issues
per Year
24
Founder Akadémiai Kiadó
Founder's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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