Protective Effect of Bergapten against Human Erythrocyte Hemolysis and Protein Denaturation In Vitro

Abstract

Bergapten, a furocoumarin found in many medicinal plants, is used for the management of various conditions. The present in vitro study evaluated the ability of bergapten to prevent human erythrocyte hemolysis and protein denaturation. Bergapten administered at 10, 30, and 100 μg/ml exhibited a significant concentration-dependent protection on the erythrocyte membrane exposed to hypotonicity and heat-induced hemolysis. The concentration at which bergapten inhibited 50% of the cells from hemolysis (IC50) was determined on a dose-response curve, plotted as logarithmic (concentration) against percentage inhibition, keeping the hemolysis produced within the control group at 100%. Bergapten treatment produced an IC50 value of 7.71 ± 0.27 μg/ml and 4.23 ± 0.42 μg/ml for hypotonicity and heat-induced hemolysis, respectively. Diclofenac sodium at similar concentrations produced an IC50 value of 12.22 ± 0.30 μg/ml and 9.44 ± 0.23 μg/ml in the hypotonicity and heat-induced hemolysis, respectively. The ability of bergapten to inhibit protein denaturation was studied as part of an investigation on its mechanism of action. The results showed a significant concentration-dependent reduction in protein denaturation. When administered at 10, 30, and 100 μg/ml, bergapten produced a concentration-dependent reduction in albumin denaturation. Bergapten inhibited protein denaturation with IC50 values of 5.34 ± 0.30 μg/ml and 12.18 ± 0.20 μg/ml in the heat-treated egg albumin and bovine serum albumin denaturation experiments, respectively. Diclofenac sodium (10, 30, and 100 μg/ml) exhibited a similar protection against heat-treated egg albumin and bovine serum albumin denaturation experiments with IC50 values of 8.93 ± 0.17 μg/ml and 12.72 ± 0.11 μg/ml, respectively. Taken together, data from this study show that the pharmacological properties of bergapten may in part be related to its membrane-stabilizing and antidenaturation properties.

A Survey of the Bio-activity of the Fruit Rind of Kiwano (Cucumis metuliferus)

“…For instance, the denaturation of tissue proteins results in the production of autoantigens in arthritis [27,28]. Membrane proteins regulate water/volume content of the cell controlling the movement of ions such as sodium and potassium via ion channels [29]. From the result in this study, it was shown that the ethanol extract of kiwano rind inhibited denaturation of bovine albumin treated with heat in a concentration-dependent manner exhibiting 47.14% maximum activity.…”

Erythroprotective Potential of Phycobiliproteins Extracted from Porphyridium cruentum

“…The stability of the erythrocyte membrane can be extrapolated to the stabilization of the lysosomal membrane, due to its absence of organelles and similarity to the cell membrane [ 104 ]. During the inflammatory process, leukocytes and neutrophils release lysosomal enzymes towards the inflammation sites [ 105 , 106 ], and these can generate persistent inflammation and tissue damage, threatening human health. The osmosis effect of vascularization during inflammation is reproduced by the hypotonic solution, an analysis where the stabilization of the RBC membranes represents the lysosomal membranes, whose importance lies in limiting the inflammatory response by preventing the release of lysosomal enzymes.…”

In Vitro Antioxidant, Anti-Inflammatory, and Digestive Enzymes Inhibition Activities of Hydro-Ethanolic Leaf and Bark Extracts of Psychotria densinervia (K. Krause) Verdc

“…erefore, any agent that can prevent protein denaturation is worth considering for anti-inflammatory drug development. Most nonsteroidal anti-inflammatory drugs (NSAIDs) are known to possess the intrinsic ability to stabilize or prevent heat-treated albumin denaturation at physiological pH 6.2-6.5 [35,37]. Also, it has been reported that the administration of NSAIDs to overweight patients may improve the loss in their body weight [38].…”