Evidence for the Binding of Synthetic Cannabinoids to Human and Bovine Serum Albumin

Albumin is the most abundant protein in blood and binds to a large variety of small molecules such as drugs, fatty acids, and other organic compounds. The distribution and overall concentrations of some drugs in blood have been proposed to be affected by albumin because otherwise poorly soluble compounds may circulate in larger amounts by being bound to albumin. Synthetic cannabinoids comprise over 200 compounds with low aqueous solubility that bind and activate integral membrane cannabinoid receptors in the brain and other tissues. Although synthetic cannabinoid use is global and has been associated with serious side effects there is limited information on factors affecting their toxicity. It is hypothesized that despite their diversity of structures, synthetic cannabinoids bind to serum albumin and this renders them more soluble in plasma. The goal of the current research was to test for the formation of complexes between synthetic cannabinoids and albumin by using electrophoresis, uv‐vis and fluorescence spectroscopy. In the presence but not in the absence of BSA, fluorescent bands at the position of albumin were seen for mixtures of human serum and bovine serum albumin with Bay 59–3074 and JWH‐015, Nile Red, timolol, coumarin and eosin. In the absence of these compounds, the albumin band was not fluorescent or colored. The colors of eosin, bromophenol blue and Nile red changed in the presence of albumin indicating an influence of albumin on the spectral properties of small compounds. The binding of compounds to albumin was further examined and demonstrated by by uv‐vis and fluorescence spectroscopy. It was concluded that the binding of synthetic cannabinoids to serum albumin was observed for the first time. It was also shown that agarose gel electrophoresis can be used in a novel fashion to detect the interaction of certain colored or fluorescent compounds with albumin. Support or Funding Information Center for Undergraduate Research, Albany State University This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .