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18th ISAD

International Symposium on Albumin Dialysis

Analysis of Albumin function by investigating conformational mobility

Albumin is the major plasma protein, it is a very flexible molecule with seven known binding sites for long chain fatty acids, which differ in their binding affinity. It´s well known physiological functions beside others are the maintenance of osmotic pressure and the transport function for fatty acids and other hydrophobic substances, trace elements and also medical drugs. Binding of these molecules can affect the ability of conformational mobility of human serum albumin. Also the detoxification is an important function of serum albumin, pathophysiological changes can influence this functionality. This albumin function correlates to dangerous illnesses like sepsis or liver failure. Serum albumin removes metabolites and toxins by transport to the liver, to help the organism to detoxify and regenerate.

The Albumin-functionality-test based on EPR spectroscopy can detect these modified binding and functional characteristics of serum albumin. The used radical supporting spin probe binds analogous other natural albumin ligands variably strong in different albumin binding sites and thus serves as indirect marker for the serum albumin functionality.

Due to a comparison of three different mixtures of albumin and a spin labeled fatty acid the Albumin-functionality-test simulate binding, transport and release conditions in vitro. Thus an “effective” albumin concentration could be determined, which quantifies the amount of functional albumin in the patient in comparison to healthy population. As a conclusion of results of various modules the Albumin-functionality-test can be used for disease progression monitoring and prognosis of sepsis and liver diseases, for examination of efficiency of liver dialysis systems and for quality control of commercial albumins.

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