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• W4385688431 abstract "Albumin as the most abundant plasma protein represents a target structure for both drug and physicochemical therapeutic approaches to eliminate uremic toxins more efficiently. Potentially, this approach could reduce mortality of haemodialysis patients. However, little is known about albumin functional properties in these patients and its alteration by haemodialysis treatment.Binding and detoxification efficiency of albumin were assessed by electron paramagnetic resonance spectroscopy using a spin-labelled fatty acid. Binding efficiency (BE) reflects strength and amount of bound fatty acids under certain ethanol concentration. Detoxification efficiency (DTE) reflects the molecular flexibility of the patient's albumin molecule, thus the ability of changing the conformation depending on ethanol concentration. Percentage of BE and DTE are depicted in relation to healthy individuals [100%].58 patients (59% male, median age 68 years, median time on haemodialysis 32 months) were included in the study. Before haemodialysis treatment, albumin binding and detoxification efficiency were substantially below healthy individuals (median BE 52% (IQR 45-59%); median DTE 38% (IQR 32-49%)). After haemodialysis treatment, median BE and DTE significantly decreased (BE 28% (IQR 20-41%); DTE 11% (IQR 7-27%; P < 0.001)). BE and DTE decline after haemodialysis was not dependent on age, sex or treatment modalities but to a certain extent on the level of non-esterified fatty acids.Albumin binding and detoxification efficiency of fatty acids in maintenance haemodialysis patients were substantially below that in healthy individuals and even declined after dialysis treatment. These findings might be helpful when considering new therapeutic approaches in maintenance haemodialysis patients." @default.
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• W4385688431 date "2023-08-09" @default.
• W4385688431 modified "2023-10-14" @default.
• W4385688431 title "Binding and detoxification efficiency of albumin decline after haemodialysis" @default.
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• W4385688431 doi "https://doi.org/10.1093/ndt/gfad133" @default.
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