Thermal Stabilization of Tumor Necrosis Factor‐α and C‐Reactive Protein by Compatible Solutes

Prokaryotic and Eukaryotic organisms are known to respond to various forms of stress by increasing intracellular concentrations of small organic compounds, called compatible solutes. These compounds increase survival in response to extremes of osmolarity, pH, temperature, desiccation and chemical denaturants. The protective properties of these compounds are largely the result of the stabilization of cellular macromolecules, and significant progress has been made in elucidating the mechanisms by which this stability is conferred. Compatible solutes belong to multiple chemical classes, with differing protective properties that appear to be stress‐specific and likely with various degrees of target specificity. Here we describe initial screening efforts to quantify the thermal stabilization properties of two prominent classes of compatible solutes, small carbohydrates and amino acids. Two model proteins of diagnostic significance were chosen for these studies: tumor necrosis factor (TNF) and C‐reactive protein (CRP). These data indicate that specific members of these molecular classes within certain concentration ranges confer significant thermal stabilization to each of these proteins. These findings present interesting possibilities for future improvements in the field of medical diagnostics, specifically in the area of patient sample collection and transport where the stabilization of low concentration, labile proteins is a major concern.