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Binding studies of synthetic cathinones to human serum albumin by high-performance affinity chromatography.
Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences 2023 July 20
The binding affinity to human serum albumin (HSA) of a series of fourteen synthetic cathinones, new psychoactive substances widely abused, was investigated by high-performance affinity chromatography (HPAC). Zonal elution experiments were conducted to measure the retention times of each synthetic cathinone on an HSA column, which enabled the calculation of the percentage of the drug bound. For some synthetic cathinones, enantioselectivity on HSA was found. To gather information on the HSA binding sites and better understand the chiral recognition mechanisms, enantioresolution of selected cathinones was carried out at a milligram scale through liquid chromatography (LC) with carbamate polysaccharide-based columns. This work was followed by zonal displacement chromatography using known competitors with specific binding sites on HSA, namely (S)-ibuprofen and warfarin. Competition was observed between the tested drugs and both competitors (except for pentedrone with warfarin), which is consistent with an allosteric competition involving a non-cooperative binding mechanism.
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