Investigating antibody interactions with a polar liquid using terahertz pulsed spectroscopy.

In this article, we use terahertz spectroscopy to study the dielectric properties of the peroxidase-conjugated affinity purified goat anti-cat immunoglobulin G and the fluorescein-conjugated affinity purified goat anti-cat immunoglobulin G when they interact with polar liquids. The influence of protein concentration, as well as presence of glycerol as a cosolvent, is determined by estimation of the effective hydration shell radius of the protein in solution. The dielectric spectra in this study are measured over the frequency range 0.1-1.3 THz and it is found that the dielectric properties are dependent on the type of the charges in the hydrogen-bonded antibodies' networks. Our results indicate that the terahertz dielectric properties of polar liquids are strongly affected by the presence of the antibody and suggest that the dielectric spectrum is particularly powerful in the study of structural and conformational properties of proteins. Therefore, terahertz spectroscopy is a very sensitive approach to investigate structural features of biological systems.