Binding studies of synthetic cathinones to human serum albumin by high-performance affinity chromatography

• Type: Article in International Scientific Journal
• Date: 2023

Authors

Almeida, AS (Author) Other; Cardoso, T (Author) Other; Cravo, S (Author) Other; Tiritan M.E. (Author) FFUP; Remiao, F (Author) Other; Carla Fernandes (Author) FFUP

Journal

Title: Journal of Chromatography - Biomedical Applications

Vol. 1227

ISSN: 0378-4347

Publisher: Elsevier B.V.

Indexing

ISI Web of Knowledge - 2 Citations

Scopus - 2 Citations

Other information

Authenticus ID: P-00Y-SKX

DOI: 10.1016/j.jchromb.2023.123836

Abstract (EN): The binding affinity to human serum albumin (HSA) of a series of fourteen synthetic cathinones, new psycho-active 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 13